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	<title>bioRxiv Channel: The Sainsbury Laboratory</title>
	<link>https://biorxiv.org</link>
	<description>
	This feed contains articles for bioRxiv Channel "The Sainsbury Laboratory"
	</description>

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	<prism:publicationName>bioRxiv</prism:publicationName>
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	<title>bioRxiv</title>
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	<link>https://biorxiv.org</link>
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	<item rdf:about="https://biorxiv.org/cgi/content/short/143537v1?rss=1">
<title>
<![CDATA[
nQuire: A Statistical Framework For Ploidy Estimation Using Next Generation Sequencing 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/143537v1?rss=1"
</link>
<description><![CDATA[
SummarynQuire is a statistical framework that distinguishes between diploids, triploids and tetraploids using next generation sequencing. The command-line tool models the distribution of base frequencies at variable sites using a Gaussian Mixture Model, and uses maximum likelihood to select the most plausible ploidy model.nnAvailability and ImplementationThe model is implemented as a stand-alone Linux command line tool in the C programming language and is available at github under the MIT licence. Please also refer to github.com/clwgg/nQuire for usage instructions. Contact: clemens.weiss@tuebingen.mpg.de or hernan.burbano@tuebingen.mpg.de
]]></description>
<dc:creator>Weiss, C. L.</dc:creator>
<dc:creator>Pais, M.</dc:creator>
<dc:creator>Cano, L. M.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Burbano, H. A.</dc:creator>
<dc:date>2017-05-29</dc:date>
<dc:identifier>doi:10.1101/143537</dc:identifier>
<dc:title><![CDATA[nQuire: A Statistical Framework For Ploidy Estimation Using Next Generation Sequencing]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-05-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/130013v1?rss=1">
<title>
<![CDATA[
Pattern-Triggered Immunity And Cell Wall Integrity Maintenance Jointly Modulate Plant Stress Responses 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/130013v1?rss=1"
</link>
<description><![CDATA[
Plant cells are surrounded by walls, which must often meet opposing functional requirements during plant growth and defense. The cells meet them by modifying wall structure and composition in a tightly controlled and adaptive manner. The modifications seem to be mediated by a dedicated cell wall integrity (CWI) maintenance mechanism. Currently the mode of action of the mechanism is not understood and it is unclear how its activity is coordinated with established plant defense signaling. We investigated responses to induced cell wall damage (CWD) impairing CWI and the underlying mechanism in Arabidopsis thaliana. Interestingly inhibitor- and enzyme-derived CWD induced similar, turgor-sensitive stress responses. Genetic analysis showed that the receptor-like kinase (RLK) FEI2 and the mechano-sensitive, plasma membrane-localized Ca2+- channel MCA1 function downstream of the THE1 RLK in CWD perception. Phenotypic clustering with 27 genotypes identified a core group of RLKs and ion channels, required for activation of CWD responses. By contrast, the responses were repressed by pattern-triggered immune (PTI) signaling components including PEPR1 and 2, the receptors for the immune signaling peptide AtPep1. Interestingly AtPep1 application repressed CWD-induced phytohormone accumulation in a PEPR1/2-dependent manner. These results suggest that PTI suppresses CWD-induced defense responses through elicitor peptide-mediated signaling during defense response activation. If PTI is impaired, the suppression of CWD-induced responses is alleviated, thus compensating for defective PTI.nnSignificance statementStress resistance and plant growth determine food crop yield and efficiency of bioenergy production from ligno-cellulosic biomass. Plant cell walls are essential elements of the biological processes, therefore functional integrity of the cell walls must be maintained throughout. Here we investigate the plant cell wall integrity maintenance mechanism. We characterize its mode of action, identify essential signaling components and show that the AtPep1 signaling peptide apparently coordinates pattern triggered immunity (PTI) and cell wall integrity maintenance in plants. These results suggest how PTI and cell wall modification coordinately regulate biotic stress responses with plants possibly compensating for PTI impairment through enhanced activation of stress responses regulated by the CWI maintenance mechanism.
]]></description>
<dc:creator>Engelsdorf, T.</dc:creator>
<dc:creator>Gigli-Bisceglia, N.</dc:creator>
<dc:creator>Veerabagu, M.</dc:creator>
<dc:creator>McKenna, J. F.</dc:creator>
<dc:creator>Augstein, F.</dc:creator>
<dc:creator>van der Does, D.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Hamann, T.</dc:creator>
<dc:date>2017-04-26</dc:date>
<dc:identifier>doi:10.1101/130013</dc:identifier>
<dc:title><![CDATA[Pattern-Triggered Immunity And Cell Wall Integrity Maintenance Jointly Modulate Plant Stress Responses]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-04-26</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/146746v1?rss=1">
<title>
<![CDATA[
The ash dieback invasion of Europe was founded by two individuals from a native population with huge adaptive potential 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/146746v1?rss=1"
</link>
<description><![CDATA[
Accelerating international trade and climate change make pathogen spread an increasing concern. Hymenoscyphus fraxineus, the causal agent of ash dieback is one such pathogen, moving across continents and hosts from Asian to European ash. Most European common ash (Fraxinus excelsior) trees are highly susceptible to H. fraxineus although a small minority (~5%) evidently have partial resistance to dieback. We have assembled and annotated a draft of the H. fraxineus genome which approaches chromosome scale. Pathogen genetic diversity across Europe, and in Japan, reveals a tight bottleneck into Europe, though a signal of adaptive diversity remains in key host interaction genes (effectors). We find that the European population was founded by two divergent haploid individuals. Divergence between these haplotypes represents the 'shadow' of a large source population and subsequent introduction would greatly increase adaptive potential and the pathogen's threat. Thus, EU wide biological security measures remain an important part of the strategy to manage this disease.
]]></description>
<dc:creator>McMullan, M.</dc:creator>
<dc:creator>Rafiqi, M.</dc:creator>
<dc:creator>Kaithakottil, G.</dc:creator>
<dc:creator>Clavijo, B. J.</dc:creator>
<dc:creator>Bilham, L.</dc:creator>
<dc:creator>Orton, E.</dc:creator>
<dc:creator>Percival-Alwyn, L.</dc:creator>
<dc:creator>Ward, B. J.</dc:creator>
<dc:creator>Edwards, A.</dc:creator>
<dc:creator>Saunders, D. G. O.</dc:creator>
<dc:creator>Garcia, G.</dc:creator>
<dc:creator>Wright, J.</dc:creator>
<dc:creator>Verweij, W.</dc:creator>
<dc:creator>Koutsovoulos, G.</dc:creator>
<dc:creator>Yoshida, K.</dc:creator>
<dc:creator>Hosoya, T.</dc:creator>
<dc:creator>Williamson, L.</dc:creator>
<dc:creator>Jennings, P.</dc:creator>
<dc:creator>Ioos, R.</dc:creator>
<dc:creator>Husson, C.</dc:creator>
<dc:creator>Hietala, A. M.</dc:creator>
<dc:creator>Vivian-Smith, A.</dc:creator>
<dc:creator>Solheim, H.</dc:creator>
<dc:creator>MacLean, D.</dc:creator>
<dc:creator>Fosker, C.</dc:creator>
<dc:creator>Hall, N.</dc:creator>
<dc:creator>Brown, J. K. M.</dc:creator>
<dc:creator>Swarbreck, D.</dc:creator>
<dc:creator>Blaxter, M.</dc:creator>
<dc:creator>Downie, A.</dc:creator>
<dc:creator>Clark, M. D.</dc:creator>
<dc:date>2017-06-06</dc:date>
<dc:identifier>doi:10.1101/146746</dc:identifier>
<dc:title><![CDATA[The ash dieback invasion of Europe was founded by two individuals from a native population with huge adaptive potential]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-06-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/093773v1?rss=1">
<title>
<![CDATA[
Defining the genetic architecture of stripe rust resistance in the barley accession HOR1428 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/093773v1?rss=1"
</link>
<description><![CDATA[
Puccinia striiformis f. sp. hordei, the causal agent of barley stripe rust, is a destructive fungal pathogen that significantly affects barley cultivation. A major constraint in breeding resistant cultivars is the lack of mapping information of resistance (R) genes and their introgression into adapted germplasm. A considerable number of R genes have been described in barley to P. striiformis f. sp. hordei, but only a few loci have been mapped. Previously, Chen and Line (1999) reported two recessive seedling resistance loci in the Ethiopian landrace HOR 1428. In this study, we map two loci that confer resistance to P. striiformis f. sp. hordei in HOR 1428, which are located on chromosomes 3H and 5H. Both loci act as additive effect QTLs, each explaining approximately 20% of the phenotypic variation. We backcrossed HOR 1428 to the cv. Manchuria and selected based on markers flanking the RpsHOR128-5H locus. Saturation of the RpsHOR1428-5H locus with markers in the region found KASP marker K_1_0292 in complete coupling with resistance to P. striiformis f. sp. hordei and was designated Rps9. Isolation of Rps9 and flanking markers will facilitate the deployment of this genetic resource into existing programs for P. striiformis f. sp. hordei resistance.
]]></description>
<dc:creator>Clare, S.</dc:creator>
<dc:creator>Kitcher, W.</dc:creator>
<dc:creator>Gardiner, M.</dc:creator>
<dc:creator>Green, P.</dc:creator>
<dc:creator>Hubbard, A.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:date>2016-12-13</dc:date>
<dc:identifier>doi:10.1101/093773</dc:identifier>
<dc:title><![CDATA[Defining the genetic architecture of stripe rust resistance in the barley accession HOR1428]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2016-12-13</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/137844v1?rss=1">
<title>
<![CDATA[
An Oomycete Effector Protein Induces Shade Avoidance In Arabidopsis And Attenuates Salicylate Signaling By Binding To Host Proteins Of The RADICAL-INDUCED CELL DEATH1 Family 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/137844v1?rss=1"
</link>
<description><![CDATA[
The oomycete pathogen Hyaloperonospora arabidopsidis (Hpa) causes downy mildew disease on Arabidopsis. During infection, Hpa like other biotrophic pathogens, suppresses activation of plant innate immunity by translocating effector proteins into host cells. Some of these effectors localize to the host cell nucleus where they may manipulate transcriptional reprogramming of plant defense genes. Here we report that the nuclear-localized Hpa effector HaRxL106, when expressed in Arabidopsis, induces shade avoidance and attenuates the transcriptional response to the defense signaling molecule salicylic acid. HaRxL106 interacts with RADICAL-INDUCED CELL DEATH1 (RCD1) and loss of RCD1 function renders Arabidopsis resilient against HaRxL106-mediated suppression of immunity. To further characterize the molecular functions of RCD1 we solved a crystal structure of RCD1s Poly-(ADP-ribose)-Polymerase (PARP) domain and, based on non-conservation of amino acids constituting the active site of canonical PARPs, conclude that RCD1 has no PARP activity. We report that RCD1-type proteins are phosphorylated and identified histone-modifying Mut9-like kinases (MLKs) as RCD1-interacting proteins. A mlk1,3,4 triple mutant exhibits stronger SA-induced defense marker gene expression compared to wild-type plants. Our data suggest that HaRxL106 suppresses Arabidopsis innate immunity by manipulating the function(s) of RCD1 in the host cell nucleus and point towards a role of RCD1 as a transcriptional co-regulator that integrates signals from light and pathogen sensors.
]]></description>
<dc:creator>Wirthmueller, L.</dc:creator>
<dc:creator>Asai, S.</dc:creator>
<dc:creator>Rallapalli, G.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Fabro, G.</dc:creator>
<dc:creator>Kim, D. S.</dc:creator>
<dc:creator>Lintermann, R.</dc:creator>
<dc:creator>Jaspers, P.</dc:creator>
<dc:creator>Wrzaczek, M.</dc:creator>
<dc:creator>Kangasjarvi, J.</dc:creator>
<dc:creator>MacLean, D.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:date>2017-05-14</dc:date>
<dc:identifier>doi:10.1101/137844</dc:identifier>
<dc:title><![CDATA[An Oomycete Effector Protein Induces Shade Avoidance In Arabidopsis And Attenuates Salicylate Signaling By Binding To Host Proteins Of The RADICAL-INDUCED CELL DEATH1 Family]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-05-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/090449v1?rss=1">
<title>
<![CDATA[
NLR signaling network mediates immunity to diverse plant pathogens 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/090449v1?rss=1"
</link>
<description><![CDATA[
Plant and animal nucleotide-binding domain and leucine-rich repeat-containing (NLR) proteins often function in pairs to mediate innate immunity to pathogens. However, the degree to which NLR proteins form signaling networks beyond genetically linked pairs is poorly understood. In this study, we discovered that a large NLR immune signaling network with a complex genetic architecture confers immunity to oomycetes, bacteria, viruses, nematodes, and insects. The network emerged over 100 million years ago from a linked NLR pair that diversified into up to one half of the NLR of asterid plants. We propose that this NLR network increases robustness of immune signaling to counteract rapidly evolving plant pathogens.
]]></description>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Abd-El-Haliem, A.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Belhaj, K.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Vossen, J. H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2016-11-29</dc:date>
<dc:identifier>doi:10.1101/090449</dc:identifier>
<dc:title><![CDATA[NLR signaling network mediates immunity to diverse plant pathogens]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2016-11-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/059832v1?rss=1">
<title>
<![CDATA[
Emergence of wheat blast in Bangladesh was caused by a South American lineage of Magnaporthe oryzae 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/059832v1?rss=1"
</link>
<description><![CDATA[
In February 2016, a new fungal disease was spotted in wheat fields across eight districts in Bangladesh. The epidemic spread to an estimated 15,741 hectares, about 16% of cultivated wheat area in Bangladesh, with yield losses reaching up to 100%. Within weeks of the onset of the epidemic, we performed transcriptome sequencing of symptomatic leaf samples collected directly from Bangladeshi fields. Population genomics analyses revealed that the outbreak was caused by a wheatLinfecting South American lineage of the blast fungus Magnaporthe oryzae. We show that genomic surveillance can be rapidly applied to monitor plant disease outbreaks and provide valuable information regarding the identity and origin of the infectious agent.
]]></description>
<dc:creator>Tofazzal Islam</dc:creator>
<dc:creator>Daniel Croll</dc:creator>
<dc:creator>Pierre Gladieux</dc:creator>
<dc:creator>Darren Soanes</dc:creator>
<dc:creator>Antoine Persoons</dc:creator>
<dc:creator>Pallab Bhattacharjee</dc:creator>
<dc:creator>Shaid Hossain</dc:creator>
<dc:creator>Dipali Gupta</dc:creator>
<dc:creator>Md. Mahbubur Rahman</dc:creator>
<dc:creator>M Golam Mahboob</dc:creator>
<dc:creator>Nicola Cook</dc:creator>
<dc:creator>Moin Salam</dc:creator>
<dc:creator>Vanessa Bueno Sancho</dc:creator>
<dc:creator>Joao Nunes Maciel</dc:creator>
<dc:creator>Antonio Nani</dc:creator>
<dc:creator>Vanina Castroagudin</dc:creator>
<dc:creator>Juliana Teodora de Assis Reges</dc:creator>
<dc:creator>Paulo Ceresini</dc:creator>
<dc:creator>Sebastien Ravel</dc:creator>
<dc:creator>Ronny Kellner</dc:creator>
<dc:creator>Elisabeth Fournier</dc:creator>
<dc:creator>Didier Tharreau</dc:creator>
<dc:creator>marc-henri Lebrun</dc:creator>
<dc:creator>Bruce McDonald</dc:creator>
<dc:creator>Tim Stitt</dc:creator>
<dc:creator>Daniel Swan</dc:creator>
<dc:creator>Nicholas Talbot</dc:creator>
<dc:creator>Diane Saunders</dc:creator>
<dc:creator>Joe Win</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2016-06-19</dc:date>
<dc:identifier>doi:10.1101/059832</dc:identifier>
<dc:title><![CDATA[Emergence of wheat blast in Bangladesh was caused by a South American lineage of Magnaporthe oryzae]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2016-06-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/056242v1?rss=1">
<title>
<![CDATA[
The potato NLR immune receptor R3a does not contain non-canonical integrated domains 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/056242v1?rss=1"
</link>
<description><![CDATA[
A recent study by Kroj et al. (New Phytologist, 2016) surveyed nucleotide binding-leucine rich repeat (NLR) proteins from plant genomes for the presence of extraneous integrated domains that may serve as decoys or sensors for pathogen effectors. They reported that a FAM75 domain of unknown function occurs near the C-terminus of the potato late blight NLR protein R3a. Here, we investigated in detail the domain architecture of the R3a protein, its potato paralog R3b, and their tomato ortholog I2. We conclude that the R3a, R3b, and I2 proteins do not carry additional domains besides the classic NLR modules, and that the FAM75 domain match is likely a false positive among computationally predicted NLR-integrated domains.
]]></description>
<dc:creator>Artemis Giannakopoulou</dc:creator>
<dc:creator>Angela Chaparro-Garcia</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2016-05-31</dc:date>
<dc:identifier>doi:10.1101/056242</dc:identifier>
<dc:title><![CDATA[The potato NLR immune receptor R3a does not contain non-canonical integrated domains]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2016-05-31</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/116012v1?rss=1">
<title>
<![CDATA[
Gene expression polymorphism underpins evasion of host immunity in an asexual lineage of the Irish potato famine pathogen 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/116012v1?rss=1"
</link>
<description><![CDATA[
Outbreaks caused by asexual lineages of fungal and oomycete pathogens are an expanding threat to crops, wild animals and natural ecosystems (Fisher et al. 2012,Kupferschmidt 2012). However, the mechanisms underlying genome evolution and phenotypic plasticity in asexual eukaryotic microbes remain poorly understood (Seidl and Thomma 2014). Ever since the 19th century Irish famine, the oomycete Phytophthora infestans has caused recurrent outbreaks on potato and tomato crops that have been primarily caused by the successive rise and migration of pandemic asexual lineages (Cooke et al. 2012, Yoshida et al. 2013,Yoshida et al. 2014). Here, we reveal patterns of genomic and gene expression variation within a P. infestans asexual lineage by compared sibling strains belonging to the South American EC-1 clone that has dominated Andean populations since the 1990s (Forbes et al. 1997, Oyarzun et al. 1998, Delgado et al. 2013, Yoshida et al. 2013, Yoshida et al. 2014). We detected numerous examples of structural variation, nucleotide polymorphisms and gene conversion within the EC-1 clone. Remarkably, 17 genes are not expressed in one of the two EC-1 isolates despite apparent absence of sequence polymorphisms. Among these, silencing of an effector gene was associated with evasion of disease resistance conferred by a potato immune receptor. These results highlight the exceptional genetic and phenotypic plasticity that underpins host adaptation in a pandemic clonal lineage of a eukaryotic plant pathogen.
]]></description>
<dc:creator>Pais, M.</dc:creator>
<dc:creator>Yoshida, K.</dc:creator>
<dc:creator>Giannakopoulou, A.</dc:creator>
<dc:creator>Pel, M. A.</dc:creator>
<dc:creator>Cano, L. M.</dc:creator>
<dc:creator>Oliva, R. F.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Lindqvist-Kreuze, H.</dc:creator>
<dc:creator>Vleeshouwers, V. G. A. A.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2017-03-11</dc:date>
<dc:identifier>doi:10.1101/116012</dc:identifier>
<dc:title><![CDATA[Gene expression polymorphism underpins evasion of host immunity in an asexual lineage of the Irish potato famine pathogen]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-03-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/062026v1?rss=1">
<title>
<![CDATA[
Editing of the urease gene by CRISPR-Cas in the diatom Thalassiosira pseudonana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/062026v1?rss=1"
</link>
<description><![CDATA[
Background: CRISPR-Cas is a recent and powerful edition to the molecular toolbox which allows programmable genome editing. It has been used to modify genes in a wide variety of organisms, but only two alga to date. Here we present a methodology to edit the genome of T. pseudonana, a model centric diatom with both ecological significance and high biotechnological potential, using CRISPR-Cas.nnResults: A single construct wa assembled using Golden Gate cloning. Two sgRNAs were used to introduce a precise 37nt deletion early in the coding region of the urease gene. A high percentage of bi-allelic mutations ([&le;] 61.5%) were observed in clones with the CRISPR-Cas construct. Growth of bi-allelic mutants in urea led to a significant reduction in growth rate and cell size compared to growth in nitrate.nnConclusions: CRISPR-Cas can precisely and efficiently edit the genome of T. pseudonana. The use of Golden Gate cloning to assemble CRISPR-Cas constructs gives additional flexibility to the CRISPR-Cas method and facilitates modifications to target alternative genes or species.
]]></description>
<dc:creator>Amanda Hopes</dc:creator>
<dc:creator>Vladimir Nekrasov</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator>Thomas Mock</dc:creator>
<dc:creator></dc:creator>
<dc:date>2016-07-18</dc:date>
<dc:identifier>doi:10.1101/062026</dc:identifier>
<dc:title><![CDATA[Editing of the urease gene by CRISPR-Cas in the diatom Thalassiosira pseudonana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2016-07-18</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/032276v1?rss=1">
<title>
<![CDATA[
In planta expression screens of candidate effector proteins from the wheat yellow rust fungus reveal processing bodies as a pathogen-targeted plant cell compartment 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/032276v1?rss=1"
</link>
<description><![CDATA[
Rust fungal pathogens of wheat (Triticum spp.) affect crop yields worldwide. The molecular mechanisms underlying the virulence of these pathogens remain elusive, due to the limited availability of suitable molecular genetic research tools. Notably, the inability to perform high-throughput analyses of candidate virulence proteins (also known as effectors) impairs progress. We previously established a pipeline for the fast-forward screens of rust fungal effectors in the model plant Nicotiana benthamiana. This pipeline involves selecting candidate effectors in silico and performing cell biology and protein-protein interaction assays in planta to gain insight into the putative functions of candidate effectors. In this study, we used this pipeline to identify and characterize sixteen candidate effectors from the wheat yellow rust fungal pathogen Puccinia striiformis f sp tritici. Nine candidate effectors targeted a specific plant subcellular compartment or protein complex, providing valuable information on their putative functions in plant cells. One candidate effector, PST02549, accumulated in processing bodies (P-bodies), protein complexes involved in mRNA decapping, degradation, and storage. PST02549 also associates with the P-body-resident ENHANCER OF mRNA DECAPPING PROTEIN 4 (EDC4) from N. benthamiana and wheat. Our work identifies P-bodies as a novel plant cell compartment targeted by pathogen effectors.
]]></description>
<dc:creator>Benjamin Petre</dc:creator>
<dc:creator>Diane GO Saunders</dc:creator>
<dc:creator>Jan Sklenar</dc:creator>
<dc:creator>Cecile Lorrain</dc:creator>
<dc:creator>Ksenia V Krasileva</dc:creator>
<dc:creator>Joe Win</dc:creator>
<dc:creator>Sebastien Duplessis</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2015-11-19</dc:date>
<dc:identifier>doi:10.1101/032276</dc:identifier>
<dc:title><![CDATA[In planta expression screens of candidate effector proteins from the wheat yellow rust fungus reveal processing bodies as a pathogen-targeted plant cell compartment]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-11-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/038232v1?rss=1">
<title>
<![CDATA[
Cell re-entry assays do not support models of pathogen- independent translocation of AvrM and AVR3a effectors into plant cells 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/038232v1?rss=1"
</link>
<description><![CDATA[
The cell re-entry assay is widely used to evaluate pathogen effector protein uptake into plant cells. The assay is based on the premise that effector proteins secreted out of a leaf cell would translocate back into the cytosol of the same cell via a yet unknown host-derived uptake mechanism. Here, we critically assess this assay by expressing domains of the effector proteins AvrM-A of Melampsora lini and AVR3a of Phytophthora infestans fused to a signal peptide and fluorescent proteins in Nicotiana benthamiana. We found that the secreted fusion proteins do not re-enter plant cells from the apoplast and that the assay is prone to false-positives. We therefore emit a cautionary note on the use of the cell re-entry assay for protein trafficking studies.
]]></description>
<dc:creator>Benjamin Petre</dc:creator>
<dc:creator>Michaela Kopischke</dc:creator>
<dc:creator>Alexandre Evrard</dc:creator>
<dc:creator>Silke Robatzek</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2016-01-29</dc:date>
<dc:identifier>doi:10.1101/038232</dc:identifier>
<dc:title><![CDATA[Cell re-entry assays do not support models of pathogen- independent translocation of AvrM and AVR3a effectors into plant cells]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2016-01-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/092726v1?rss=1">
<title>
<![CDATA[
LOCALIZER: subcellular localization prediction of plant and effector proteins in the plant cell 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/092726v1?rss=1"
</link>
<description><![CDATA[
Pathogens are able to deliver effector proteins into plant cells to enable infection. Some effectors have been found to enter subcellular compartments by mimicking host targeting sequences. Although many computational methods exist to predict plant protein subcellular localization, they perform poorly for effectors. We introduce LOCALIZER for predicting plant and effector protein localization to chloroplasts, mitochondria, and nuclei. LOCALIZER shows greater prediction accuracy for chloroplast and mitochondrial targeting compared to other methods for 652 plant proteins. For 108 eukaryotic effectors, LOCALIZER outperforms other methods and predicts a previously unrecognized chloroplast transit peptide for the ToxA effector, which we show translocates into tobacco chloroplasts. Secretome-wide predictions and confocal microscopy reveal that rust fungi might have evolved multiple effectors that target chloroplasts or nuclei. LOCALIZER is the first method for predicting effector localisation in plants and is a valuable tool for prioritizing effector candidates for functional investigations. LOCALIZER is available at http://localizer.csiro.au/.
]]></description>
<dc:creator>Sperschneider, J.</dc:creator>
<dc:creator>Catanzariti, A.-M.</dc:creator>
<dc:creator>DeBoer, K.</dc:creator>
<dc:creator>Petre, B.</dc:creator>
<dc:creator>Gardiner, D.</dc:creator>
<dc:creator>Singh, K.</dc:creator>
<dc:creator>Dodds, P.</dc:creator>
<dc:creator>Taylor, J.</dc:creator>
<dc:date>2016-12-09</dc:date>
<dc:identifier>doi:10.1101/092726</dc:identifier>
<dc:title><![CDATA[LOCALIZER: subcellular localization prediction of plant and effector proteins in the plant cell]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2016-12-09</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/035006v1?rss=1">
<title>
<![CDATA[
Arabidopsis late blight: Infection of a nonhost plant by Albugo laibachii enables full colonization by Phytophthora infestans 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/035006v1?rss=1"
</link>
<description><![CDATA[
The oomycete pathogen Phytophthora infestans causes potato late blight, and as a potato and tomato specialist pathogen, is seemingly poorly adapted to infect plants outside the Solanaceae. Here, we report the unexpected finding that P. infestans can infect Arabidopsis thaliana when another oomycete pathogen, Albugo laibachii, has colonized the host plant. The behaviour and speed of P. infestans infection in Arabidopsis pre-infected with A. laibachii resemble P. infestans infection of susceptible potato plants. Transcriptional profiling of P. infestans genes during infection revealed a significant overlap in the sets of secreted-protein genes that are induced in P. infestans upon colonisation of potato and susceptible Arabidopsis, suggesting major similarities in P. infestans gene expression dynamics on the two plant species. Furthermore, we found haustoria of A. laibachii and P. infestans within the same Arabidopsis cells. This Arabidopsis - A. laibachii - P. infestans tripartite interaction opens up various possibilities to dissect the molecular mechanisms of P. infestans infection and the processes occurring in co-infected Arabidopsis cells.
]]></description>
<dc:creator>Khaoula Belhaj</dc:creator>
<dc:creator>Liliana M. Cano</dc:creator>
<dc:creator>David C. Prince</dc:creator>
<dc:creator>Ariane Kemen</dc:creator>
<dc:creator>Kentaro Yoshida</dc:creator>
<dc:creator>Yasin F. Dagdas</dc:creator>
<dc:creator>Graham J. Etherington</dc:creator>
<dc:creator>Henk-jan Schoonbeek</dc:creator>
<dc:creator>H. Peter van Esse</dc:creator>
<dc:creator>Jonathan DG Jones</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator>Sebastian Schornack</dc:creator>
<dc:creator></dc:creator>
<dc:date>2015-12-23</dc:date>
<dc:identifier>doi:10.1101/035006</dc:identifier>
<dc:title><![CDATA[Arabidopsis late blight: Infection of a nonhost plant by Albugo laibachii enables full colonization by Phytophthora infestans]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-12-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/102996v1?rss=1">
<title>
<![CDATA[
Host autophagosomes are diverted to a plant-pathogen interface 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/102996v1?rss=1"
</link>
<description><![CDATA[
Filamentous plant pathogens and symbionts invade their host cells but remain enveloped by host-derived membranes. The mechanisms underlying the biogenesis and functions of these host-microbe interfaces are poorly understood. Recently, we showed that PexRD54, an effector from the Irish potato famine pathogen Phytophthora infestans, binds host protein ATG8CL to stimulate autophagosome formation and deplete the selective autophagy receptor Joka2 from ATG8CL complexes. Here, we show that during P. infestans infection, ATG8CL autophagosomes are diverted to the pathogen interface. Our findings are consistent with the view that the pathogen coopts host selective autophagy for its own benefit.
]]></description>
<dc:creator>Dagdas, Y.</dc:creator>
<dc:creator>Pandey, P.</dc:creator>
<dc:creator>Sanguankiattichai, N.</dc:creator>
<dc:creator>Tumtas, Y.</dc:creator>
<dc:creator>Belhaj, K.</dc:creator>
<dc:creator>Duggan, C.</dc:creator>
<dc:creator>Segretin, M.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:date>2017-01-30</dc:date>
<dc:identifier>doi:10.1101/102996</dc:identifier>
<dc:title><![CDATA[Host autophagosomes are diverted to a plant-pathogen interface]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-01-30</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/087387v1?rss=1">
<title>
<![CDATA[
Genomic Rearrangements Considered as Quantitative Traits 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/087387v1?rss=1"
</link>
<description><![CDATA[
To understand the population genetics of structural variants (SVs), and their effects on phenotypes, we developed an approach to mapping SVs, particularly transpositions, segregating in a sequenced population, and which avoids calling SVs directly. The evidence for a potential SV at a locus is indicated by variation in the counts of short-reads that map anomalously to the locus. These SV traits are treated as quantitative traits and mapped genetically, analogously to a gene expression study. Association between an SV trait at one locus and genotypes at a distant locus indicate the origin and target of a transposition. Using ultra-low-coverage (0.3x) population sequence data from 488 recombinant inbred Arabidopsis genomes, we identified 6,502 segregating SVs. Remarkably, 25% of these were transpositions. Whilst many SVs cannot be delineated precisely, PCR validated 83% of 44 predicted transposition breakpoints. We show that specific SVs may be causative for quantitative trait loci for germination, fungal disease resistance and other phenotypes. Further we show that the phenotypic heritability attributable to sequence anomalies differs from, and in the case of time to germination and bolting, exceeds that due to standard genetic variation. Gene expression within SVs is also more likely to be silenced or dysregulated. This approach is generally applicable to large populations sequenced at low-coverage, and complements the prevalent strategy of SV discovery in fewer individuals sequenced at high coverage.
]]></description>
<dc:creator>Imprialou, M.</dc:creator>
<dc:creator>Kahles, A.</dc:creator>
<dc:creator>Steffen, J. B.</dc:creator>
<dc:creator>Osborne, E. J.</dc:creator>
<dc:creator>Gan, X.</dc:creator>
<dc:creator>Lempe, J.</dc:creator>
<dc:creator>Bhomra, A.</dc:creator>
<dc:creator>Belfield, E. J.</dc:creator>
<dc:creator>Visscher, A.</dc:creator>
<dc:creator>Greenhalgh, R.</dc:creator>
<dc:creator>Harberd, N. P.</dc:creator>
<dc:creator>Goram, R.</dc:creator>
<dc:creator>Hein, J. J.</dc:creator>
<dc:creator>Robert-Seilaniantz, A.</dc:creator>
<dc:creator>Jones, J. J.</dc:creator>
<dc:creator>Stegle, O.</dc:creator>
<dc:creator>Kover, P. X.</dc:creator>
<dc:creator>Tsiantis, M.</dc:creator>
<dc:creator>Nordborg, M.</dc:creator>
<dc:creator>Ratsch, G.</dc:creator>
<dc:creator>Clark, R.</dc:creator>
<dc:creator>Mott, R.</dc:creator>
<dc:date>2016-11-12</dc:date>
<dc:identifier>doi:10.1101/087387</dc:identifier>
<dc:title><![CDATA[Genomic Rearrangements Considered as Quantitative Traits]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2016-11-12</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/019521v1?rss=1">
<title>
<![CDATA[
RUST FUNGAL EFFECTORS MIMIC HOST TRANSIT PEPTIDES TO TRANSLOCATE INTO CHLOROPLASTS 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/019521v1?rss=1"
</link>
<description><![CDATA[
Parasite effector proteins target various host cell compartments to alter host processes and promote infection. How effectors cross membrane-rich interfaces to reach these compartments is a major question in effector biology. Growing evidence suggests that effectors use molecular mimicry to subvert host cell machinery for protein sorting. We recently identified CTP1 (chloroplast-targeted protein 1), a candidate effector from the poplar leaf rust fungus Melampsora larici-populina that carries a predicted transit peptide and accumulates in chloroplasts. Here, we show that the CTP1 transit peptide is necessary and sufficient for accumulation in the stroma of chloroplasts, and is cleaved after translocation. CTP1 is part of a Melampsora-specific family of polymorphic secreted proteins whose members translocate and are processed in chloroplasts in a N-terminal signal-dependent manner. Our findings reveal that fungi have evolved effector proteins that mimic plant-specific sorting signals to traffic within plant cells.
]]></description>
<dc:creator>Benjamin Petre</dc:creator>
<dc:creator>Cécile Lorrain</dc:creator>
<dc:creator>Diane Saunders</dc:creator>
<dc:creator>Sébastien Duplessis</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2015-05-19</dc:date>
<dc:identifier>doi:10.1101/019521</dc:identifier>
<dc:title><![CDATA[RUST FUNGAL EFFECTORS MIMIC HOST TRANSIT PEPTIDES TO TRANSLOCATE INTO CHLOROPLASTS]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-05-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/022079v1?rss=1">
<title>
<![CDATA[
Tomato I2 immune receptor can be engineered to confer partial resistance to the oomycete Phytophthora infestans in addition to the fungus Fusarium oxysporum 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/022079v1?rss=1"
</link>
<description><![CDATA[
Plants and animals rely on immune receptors, known as nucleotide-binding domain and leucine-rich repeat containing proteins (NB-LRR or NLR), to defend against invading pathogens and activate immune responses. How NLR receptors respond to pathogens is inadequately understood. We previously reported single-residue mutations that expand the response of the potato immune receptor R3a to AVR3aEM, a stealthy effector from the late blight oomycete pathogen Phytophthora infestans. I2, another NLR that mediates resistance to the wilt causing fungus Fusarium oxysporum f. sp. lycopersici, is the tomato ortholog of R3a. We transferred previously identified R3a mutations to I2 to assess the degree to which the resulting I2 mutants have an altered response. We discovered that wild-type I2 protein responds weakly to AVR3a. One mutant in the N-terminal coiled-coil domain, I2I141N, appeared sensitized and displayed markedly increased response to AVR3a. Remarkably, I2I141N conferred partial resistance to P. infestans. Further, I2I141N has an expanded response spectrum to F. oxysporum f. sp. lycopersici effectors compared to the wild-type I2 protein. Our results suggest that synthetic immune receptors can be engineered to confer resistance to phylogenetically divergent pathogens and indicate that knowledge gathered for one NLR could be exploited to improve NLRs from other plant species.
]]></description>
<dc:creator>Artemis Giannakopoulou</dc:creator>
<dc:creator>John F. C. Steele</dc:creator>
<dc:creator>Maria Eugenia Segretin</dc:creator>
<dc:creator>Tolga O. Bozkurt</dc:creator>
<dc:creator>Ji Zhou</dc:creator>
<dc:creator>Silke Robatzek</dc:creator>
<dc:creator>Mark J. Banfield</dc:creator>
<dc:creator>Marina Pais</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2015-07-07</dc:date>
<dc:identifier>doi:10.1101/022079</dc:identifier>
<dc:title><![CDATA[Tomato I2 immune receptor can be engineered to confer partial resistance to the oomycete Phytophthora infestans in addition to the fungus Fusarium oxysporum]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-07-07</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/100834v1?rss=1">
<title>
<![CDATA[
Immune receptors with exogenous domain fusions form evolutionary hotspots in grass genomes 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/100834v1?rss=1"
</link>
<description><![CDATA[
BackgroundThe plant immune system is innate, encoded in the germline. Using it efficiently, plants are capable of recognizing a diverse range of rapidly evolving pathogens. A recently described phenomenon shows that plant immune receptors are able to recognize pathogen effectors through the acquisition of exogenous protein domains from other plant genes.nnResultsWe showed that plant immune receptors with integrated domains are distributed unevenly across their phylogeny in grasses. Using phylogenetic analysis, we uncovered a major integration clade, whose members underwent repeated independent integration events producing diverse fusions. This clade is ancestral in grasses with members often found on syntenic chromosomes. Analyses of these fusion events revealed that homologous receptors can be fused to diverse domains. Furthermore, we discovered a 43 amino acids long motif that was associated with this dominant integration clade and was located immediately upstream of the fusion site. Sequence analysis revealed that DNA transposition and/or ectopic recombination are the most likely mechanisms of NLR-ID formation.nnConclusionsThe identification of this subclass of plant immune receptors that is naturally adapted to new domain integration will inform biotechnological approaches for generating synthetic receptors with novel pathogen  baits.
]]></description>
<dc:creator>Bailey, P. C.</dc:creator>
<dc:creator>Dagdas, G.</dc:creator>
<dc:creator>Baggs, E.</dc:creator>
<dc:creator>Haerty, W.</dc:creator>
<dc:creator>Krasileva, K. V.</dc:creator>
<dc:date>2017-01-20</dc:date>
<dc:identifier>doi:10.1101/100834</dc:identifier>
<dc:title><![CDATA[Immune receptors with exogenous domain fusions form evolutionary hotspots in grass genomes]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-01-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/004507v1?rss=1">
<title>
<![CDATA[
Using 2k + 2 bubble searches to find SNPs in k-mer graphs 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/004507v1?rss=1"
</link>
<description><![CDATA[
This preprint is now available in published form as:  Using 2k + 2 bubble searches to find SNPs in k-mer graphs, Reda Younsi; Dan MacLean, Bioinformatics 2014; doi: 10.1093/bioinformatics/btu706nnSingle Nucleotide Polymorphism (SNP) discovery is an important preliminary for understanding genetic variation. With current sequencing methods we can sample genomes comprehensively. SNPs are found by aligning sequence reads against longer assembled references. De Bruijn graphs are efficient data structures that can deal with the vast amount of data from modern technologies. Recent work has shown that the topology of these graphs captures enough information to allow the detection and characterisation of genetic variants, offering an alternative to alignment-based methods. Such methods rely on depth-first walks of the graph to identify closing bifurcations. These methods are conservative or generate many false-positive results, particularly when traversing highly inter-connected (complex) regions of the graph or in regions of very high coverage.We devised an algorithm that calls SNPs in converted De Bruijn graphs by enumerating 2k + 2 cycles. We evaluated the accuracy of predicted SNPs by comparison with SNP lists from alignment based methods. We tested accuracy of the SNP calling using sequence data from sixteen ecotypes of Arabidopsis thaliana and found that accuracy was high. We found that SNP calling was even across the genome and genomic feature types. Using sequence based attributes of the graph to train a decision tree allowed us to increase accuracy of SNP calls further.Together these results indicate that our algorithm is capable of finding SNPs accurately in complex sub-graphs and potentially comprehensively from whole genome graphs.The source code for a C++ implementation of our algorithm is available under the GNU Public Licence v3 at:https://github.com/redayounsi/2kplus2
]]></description>
<dc:creator>Reda Younsi</dc:creator>
<dc:creator>Dan MacLean</dc:creator>
<dc:creator></dc:creator>
<dc:date>2014-04-24</dc:date>
<dc:identifier>doi:10.1101/004507</dc:identifier>
<dc:title><![CDATA[Using 2k + 2 bubble searches to find SNPs in k-mer graphs]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2014-04-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/021774v1?rss=1">
<title>
<![CDATA[
The two-speed genomes of filamentous pathogens: waltz with plants 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/021774v1?rss=1"
</link>
<description><![CDATA[
Fungi and oomycetes include deep and diverse lineages of eukaryotic plant pathogens. The last 10 years have seen the sequencing of the genomes of a multitude of species of these so-called filamentous plant pathogens. Already, fundamental concepts have emerged. Filamentous plant pathogen genomes tend to harbor large repertoires of genes encoding virulence effectors that modulate host plant processes. Effector genes are not randomly distributed across the genomes but tend to be associated with compartments enriched in repetitive sequences and transposable elements. These findings have led to the "two-speed genome" model in which filamentous pathogen genomes have a bipartite architecture with gene sparse, repeat rich compartments serving as a cradle for adaptive evolution. Here, we review this concept and discuss how plant pathogens are great model systems to study evolutionary adaptations at multiple time scales. We will also introduce the next phase of research on this topic.
]]></description>
<dc:creator>Suomeng Dong</dc:creator>
<dc:creator>Sylvain Raffaele</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2015-07-01</dc:date>
<dc:identifier>doi:10.1101/021774</dc:identifier>
<dc:title><![CDATA[The two-speed genomes of filamentous pathogens: waltz with plants]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-07-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/019471v1?rss=1">
<title>
<![CDATA[
The Cf-4 receptor-like protein associates with the BAK1 receptor-like kinase to initiate receptor endocytosis and plant immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/019471v1?rss=1"
</link>
<description><![CDATA[
O_LIThe first layer of plant immunity is activated by cell surface receptor-like kinases (RLKs) and proteins (RLPs) that detect infectious pathogens. Constitutive interaction with the RLK SUPPRESSOR OF BIR1 (SOBIR1) contributes to RLP stability and kinase activity. As RLK activation requires transphosphorylation with a second associated RLK, it remains elusive how RLPs initiate downstream signaling. To address this, we investigated functioning of Cf RLPs that mediate immunity of tomato against Cladosporium fulvum.nC_LIO_LIWe employed live-cell imaging and co-immunoprecipitation in tomato and Nicotiana benthamiana to investigate the requirement of associated kinases for Cf activity and ligand-induced subcellular trafficking of Cf-4.nC_LIO_LIUpon elicitation with the matching effector ligands Avr4 and Avr9, BRI1-ASSOCIATED KINASE 1 (BAK1) associates with Cf-4 and Cf-9. Furthermore, Cf-4 that interacts with SOBIR1 at the plasma membrane, is recruited to late endosomes after elicitation. Significantly, BAK1 is required for Avr4-triggered endocytosis, effector-triggered defenses in Cf-4 plants and resistance of tomato against C. fulvum.nC_LIO_LIOur observations indicate that RLP-mediated immune signaling and endocytosis require ligand-induced recruitment of BAK1, reminiscent of BAK1 interaction and subcellular fate of the FLAGELLIN SENSING 2 RLK. This reveals that diverse classes of cell surface immune receptors share common requirements for signaling initiation and endocytosis.nC_LI
]]></description>
<dc:creator>Jelle Postma</dc:creator>
<dc:creator>Thomas W. H. Liebrand</dc:creator>
<dc:creator>Guozhi Bi</dc:creator>
<dc:creator>Alexandre Evrard</dc:creator>
<dc:creator>Ruby R. Bye</dc:creator>
<dc:creator>Malick Mbengue</dc:creator>
<dc:creator>Matthieu H. A. J. Joosten</dc:creator>
<dc:creator>Silke Robatzek</dc:creator>
<dc:creator></dc:creator>
<dc:date>2015-05-19</dc:date>
<dc:identifier>doi:10.1101/019471</dc:identifier>
<dc:title><![CDATA[The Cf-4 receptor-like protein associates with the BAK1 receptor-like kinase to initiate receptor endocytosis and plant immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-05-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/015479v1?rss=1">
<title>
<![CDATA[
The NLR helper protein NRC3 but not NRC1 is required for Pto-mediated cell death in Nicotiana benthamiana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/015479v1?rss=1"
</link>
<description><![CDATA[
Intracellular immune receptors of the nucleotide-binding leucine-rich repeat (NB-LRR or NLR) proteins often function in pairs, with "helper" proteins required for the activity of "sensors" that mediate pathogen recognition. The NLR helper NRC1 (NB-LRR protein required for HR-associated cell death 1) has been described as a signalling hub required for the cell death mediated by both cell surface and intracellular immune receptors in the model plant Nicotiana benthamiana. However, this work predates the availability of the N. benthamiana genome and whether NRC1 is indeed required for the reported phenotypes has not been confirmed. Here, we investigated the NRC family of solanaceous plants using a combination of genome annotation, phylogenetics, gene silencing and genetic complementation experiments. We discovered that a paralog of NRC1, we termed NRC3, is required for the hypersensitive cell death triggered by the disease resistance protein Pto but not Rx and Mi-1.2. NRC3 may also contribute to the hypersensitive cell death triggered by the receptor-like protein Cf-4. Our results highlight the importance of applying genetic complementation to validate gene function in RNA silencing experiments.
]]></description>
<dc:creator>Chih-Hang Wu</dc:creator>
<dc:creator>Khaoula Belhaj</dc:creator>
<dc:creator>Tolga O. Bozkurt</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2015-02-19</dc:date>
<dc:identifier>doi:10.1101/015479</dc:identifier>
<dc:title><![CDATA[The NLR helper protein NRC3 but not NRC1 is required for Pto-mediated cell death in Nicotiana benthamiana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-02-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/018978v1?rss=1">
<title>
<![CDATA[
Sequencing of 15,622 gene-bearing BACs reveals new features of the barley genome 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/018978v1?rss=1"
</link>
<description><![CDATA[
Barley (Hordeum vulgare L.) possesses a large and highly repetitive genome of 5.1 Gb that has hindered the development of a complete sequence. In 2012, the International Barley Sequencing Consortium released a resource integrating whole-genome shotgun sequences with a physical and genetic framework. However, since only 6,278 BACs in the physical map were sequenced, detailed fine structure was limited. To gain access to the gene-containing portion of the barley genome at high resolution, we identified and sequenced 15,622 BACs representing the minimal tiling path of 72,052 physical mapped gene-bearing BACs. This generated about 1.7 Gb of genomic sequence containing 17,386 annotated barley genes. Exploration of the sequenced BACs revealed that although distal ends of chromosomes contain most of the gene-enriched BACs and are characterized by high rates of recombination, there are also gene-dense regions with suppressed recombination. Knowledge of these deviant regions is relevant to trait introgression, genome-wide association studies, genomic selection model development and map-based cloning strategies. Sequences and their gene and SNP annotations can be accessed and exported via http://harvest-web.org/hweb/utilmenu.wc or through the software HarvEST:Barley (download from harvest.ucr.edu). In the latter, we have implemented a synteny viewer between barley and Aegilops tauschii to aid in comparative genome analysis.
]]></description>
<dc:creator>María Muñoz-Amatriaín</dc:creator>
<dc:creator>Stefano Lonardi</dc:creator>
<dc:creator>MingCheng Luo</dc:creator>
<dc:creator>Kavitha Madishetty</dc:creator>
<dc:creator>Jan Svensson</dc:creator>
<dc:creator>Matthew Moscou</dc:creator>
<dc:creator>Steve Wanamaker</dc:creator>
<dc:creator>Tao Jiang</dc:creator>
<dc:creator>Andris Kleinhofs</dc:creator>
<dc:creator>Gary Muehlbauer</dc:creator>
<dc:creator>Roger Wise</dc:creator>
<dc:creator>Nils Stein</dc:creator>
<dc:creator>Yaqin Ma</dc:creator>
<dc:creator>Edmundo Rodriguez</dc:creator>
<dc:creator>Dave Kudrna</dc:creator>
<dc:creator>Prasanna R Bhat</dc:creator>
<dc:creator>Shiaoman Chao</dc:creator>
<dc:creator>Pascal Condamine</dc:creator>
<dc:creator>Shane Heinen</dc:creator>
<dc:creator>Josh Resnik</dc:creator>
<dc:creator>Rod Wing</dc:creator>
<dc:creator>Heather N Witt</dc:creator>
<dc:creator>Matthew Alpert</dc:creator>
<dc:creator>Marco Beccuti</dc:creator>
<dc:creator>Serdar Bozdag</dc:creator>
<dc:creator>Francesca Cordero</dc:creator>
<dc:creator>Hamid Mirebrahim</dc:creator>
<dc:creator>Rachid Ounit</dc:creator>
<dc:creator>Yonghui Wu</dc:creator>
<dc:creator>Frank You</dc:creator>
<dc:creator>Jie Zheng</dc:creator>
<dc:creator>Hana Šimková</dc:creator>
<dc:creator>Jaroslav Doležel</dc:creator>
<dc:creator>Jane Grimwood</dc:creator>
<dc:creator>Jeremy Schmutz</dc:creator>
<dc:creator>Denisa Duma</dc:creator>
<dc:creator>Lothar Altschmied</dc:creator>
<dc:creator>Tom Blake</dc:creator>
<dc:creator>Phil Bregitzer</dc:creator>
<dc:creator>Laurel Cooper</dc:creator>
<dc:creator>Muharrem Dilbirligi</dc:creator>
<dc:creator>Anders Falk</dc:creator>
<dc:creator>Lei</dc:creator>
<dc:date>2015-05-05</dc:date>
<dc:identifier>doi:10.1101/018978</dc:identifier>
<dc:title><![CDATA[Sequencing of 15,622 gene-bearing BACs reveals new features of the barley genome]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-05-05</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/026856v1?rss=1">
<title>
<![CDATA[
IDENTIFICATION OF GENOMIC REGIONS CARRYING A CAUSAL MUTATION IN UNORDERED GENOMES 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/026856v1?rss=1"
</link>
<description><![CDATA[
Whole genome sequencing using high-throughput sequencing (HTS) technologies offers powerful opportunities to study genetic variation. Mapping the mutations responsible for different phenotypes is generally an involved and time-consuming process so researchers have developed user-friendly tools for mapping-by-sequencing, yet they are not applicable to organisms with non-sequenced genomes. We introduce SDM (SNP Distribution Method), a reference independent method for rapid discovery of mutagen-induced mutations in typical forward genetic screens. SDM aims to order a disordered collection of HTS reads or contigs such that the fragment carrying the causative mutation can be identified. SDM uses typical distributions of homozygous SNPs that are linked to a phenotype-altering SNP in a non-recombinant region as a model to order the fragments. To implement and test SDM, we created model genomes with an idealised SNP density based on Arabidopsis thaliana chromosome 1 and analysed fragments with size distribution similar to reads or contigs assembled from HTS sequencing experiments. SDM groups the contigs by their normalised SNP density and arranges them to maximise the fit to the expected SNP distribution. We tested the procedure in existing datasets by examining SNP distributions in recent out-cross and back-cross experiments in Arabidopsis thaliana backgrounds. In all the examples we analysed, homozygous SNPs were normally distributed around the causal mutation. We used the real SNP densities obtained from these experiments to prove the efficiency and accuracy of SDM. The algorithm was able to successfully identify small sized (10-100 kb) genomic regions containing the causative mutation.
]]></description>
<dc:creator>Pilar Corredor-Moreno</dc:creator>
<dc:creator>Ed Chalstrey</dc:creator>
<dc:creator>Carlos A Lugo</dc:creator>
<dc:creator>Dan MacLean</dc:creator>
<dc:creator></dc:creator>
<dc:date>2015-09-15</dc:date>
<dc:identifier>doi:10.1101/026856</dc:identifier>
<dc:title><![CDATA[IDENTIFICATION OF GENOMIC REGIONS CARRYING A CAUSAL MUTATION IN UNORDERED GENOMES]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2015-09-15</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/004564v1?rss=1">
<title>
<![CDATA[
Crowdsourced analysis of ash and ash dieback through the Open Ash Dieback project: A year 1 report on datasets and analyses contributed by a self-organising community. 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/004564v1?rss=1"
</link>
<description><![CDATA[
Ash dieback is a fungal disease of ash trees caused by Hymenoscyphus pseudoalbidus that has swept across Europe in the last two decades and is a significant threat to the ash population. This emergent pathogen has been relatively poorly studied and little is known about its genetic make-up. In response to the arrival of this dangerous pathogen in the UK we took the unusual step of providing an open access database and initial sequence datasets to the scientific community for analysis prior to performing an analysis of our own. Our goal was to crowdsource genomic and other analyses and create a community analysing this pathogen. In this report on the evolution of the community and data and analysis obtained in the first year of this activity, we describe the nature and the volume of the contributions and reveal some preliminary insights into the genome and biology of H. pseudoalbidus that emerged. In particular our nascent community generated a first-pass genome assembly containing abundant collapsed AT-rich repeats indicating a typically complex genome structure. Our open science and crowdsourcing effort has brought a wealth of new knowledge about this emergent pathogen within a short time-frame. Our community endeavour highlights the positive impact that open, collaborative approaches can have on fast, responsive modern science.
]]></description>
<dc:creator>Diane Saunders</dc:creator>
<dc:creator>Kentaro Yoshida</dc:creator>
<dc:creator>Christine Sambles</dc:creator>
<dc:creator>Rachel Glover</dc:creator>
<dc:creator>Bernardo Clavijo</dc:creator>
<dc:creator>Manuel Corpas</dc:creator>
<dc:creator>Daniel Bunting</dc:creator>
<dc:creator>Suomeng Dong</dc:creator>
<dc:creator>Ghanasyam Rallapalli</dc:creator>
<dc:creator>Matthew Clark</dc:creator>
<dc:creator>David Swarbreck</dc:creator>
<dc:creator>Sarah Ayling</dc:creator>
<dc:creator>Matthew Bashton</dc:creator>
<dc:creator>Steve Collin</dc:creator>
<dc:creator>Tsuyoshi Hosoya</dc:creator>
<dc:creator>Anne Edwards</dc:creator>
<dc:creator>Lisa Crossman</dc:creator>
<dc:creator>Graham Etherington</dc:creator>
<dc:creator>Joe Win</dc:creator>
<dc:creator>Liliana Cano</dc:creator>
<dc:creator>David Studholme</dc:creator>
<dc:creator>J Allan Downie</dc:creator>
<dc:creator>Mario Caccamo</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator>Dan MacLean</dc:creator>
<dc:creator></dc:creator>
<dc:date>2014-04-25</dc:date>
<dc:identifier>doi:10.1101/004564</dc:identifier>
<dc:title><![CDATA[Crowdsourced analysis of ash and ash dieback through the Open Ash Dieback project: A year 1 report on datasets and analyses contributed by a self-organising community.]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2014-04-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/012963v1?rss=1">
<title>
<![CDATA[
Phytophthora infestans RXLR-WY effector AVR3a associates with a Dynamin-Related Protein involved in endocytosis of a plant pattern recognition receptor 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/012963v1?rss=1"
</link>
<description><![CDATA[
Perception of pathogen associated molecular patterns (PAMPs) by cell surface localized pattern recognition receptors (PPRs), activates plant basal defense responses in a process known as PAMP/PRR-triggered immunity (PTI). In turn, pathogens deploy effector proteins that interfere with different steps in PTI signaling. However, our knowledge of PTI suppression by filamentous plant pathogens, i.e. fungi and oomycetes, remains fragmentary. Previous work revealed that BAK1/SERK3, a regulatory receptor of several PRRs, contributes to basal immunity against the Irish potato famine pathogen Phytophthora infestans. Moreover BAK1/SERK3 is required for the cell death induced by P. infestans elicitin INF1, a protein with characteristics of PAMPs. The P. infestans host-translocated RXLR-WY effector AVR3a is known to supress INF1-mediated defense by binding the E3 ligase CMPG1. In contrast, AVR3aKl-Y147del, a deletion mutant of the C-terminal tyrosine of AVR3a, fails to bind CMPG1 and suppress INF1 cell death. Here we studied the extent to which AVR3a and its variants perturb additional BAK1/SERK3 dependent PTI responses using the plant PRR FLAGELLIN SENSING 2 (FLS2). We found that all tested variants of AVR3a, including AVR3aKl-Y147del, suppress early defense responses triggered by the bacterial flagellin-derived peptide flg22 and reduce internalization of activated FLS2 from the plasma membrane without disturbing its nonactivated localization. Consistent with this effect of AVR3a on FLS2 endocytosis, we discovered that AVR3a associates with the Dynamin-Related Protein DRP2, a plant GTPase implicated in receptor-mediated endocytosis. Interestingly, DRP2 is required for ligand-induced FLS2 internalization but does not affect internalization of the growth receptor BRASSINOSTEROID INSENSITIVE 1 (BRI1). Furthermore, overexpression of DRP2 suppressed accumulation of reactive oxygen species triggered by PAMP treatment. We conclude that AVR3a associates with a key cellular trafficking and membrane-remodeling complex involved in immune receptor-mediated endocytosis and signaling. AVR3a is a multifunctional effector that can suppress BAK1/SERK3 mediated immunity through at least two different pathways.nnAUTHOR SUMMARYPlants have a basal layer of immunity to mount defense responses against invading pathogens; in turn, pathogens deploy effector proteins to subvert plant immunity and manipulate host processes to enable parasitic infection. The Irish potato famine pathogen Phytophthora infestans has a large set of effectors that target multiple host cellular sites. The best-characterized P. infestans effector AVR3a supports enhanced infection and suppresses the cell death induced by the P. infestans protein INF1-elicitin. Previous work demonstrated that the plant immunity co-receptor BAK1/SERK3 contributes to basal immunity to P. infestans and that the RXLR-WY effector of P. infestans suppresses BAK1/SERK3-mediated immunity by binding the E3 ligase protein CMPG1. Here we show that AVR3a suppresses additional defense responses mediated by BAK1/SERK3 independently of CMPG1. AVR3a reduces the endocytosis of the plant receptor FLS2, which recognizes the flagellin-derived peptide flg22 in a BAK1/SERK3 dependent manner. Furthermore, we demonstrate that AVR3a associates with the Dynamin-Related Protein DRP2, a plant GTPase involved in receptor-mediated endocytosis that is required for FLS2 internalization. Our work revealed that AVR3a is a multifunctional effector that perturbs cellular trafficking initiated at the cell periphery by at least two mechanisms, and that this effector associates with a key cellular trafficking and membrane-remodeling complex involved in immune receptor-mediated endocytosis and signaling.
]]></description>
<dc:creator>Angela Chaparro-Garcia</dc:creator>
<dc:creator>Simon Schwizer</dc:creator>
<dc:creator>Jan Sklenar</dc:creator>
<dc:creator>Kentaro Yoshida</dc:creator>
<dc:creator>Jorunn I. B. Bos</dc:creator>
<dc:creator>Sebastian Schornack</dc:creator>
<dc:creator>Alexandra M. E. Jones</dc:creator>
<dc:creator>Tolga O. Bozkurt</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:creator></dc:creator>
<dc:date>2014-12-19</dc:date>
<dc:identifier>doi:10.1101/012963</dc:identifier>
<dc:title><![CDATA[Phytophthora infestans RXLR-WY effector AVR3a associates with a Dynamin-Related Protein involved in endocytosis of a plant pattern recognition receptor]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2014-12-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/006155v1?rss=1">
<title>
<![CDATA[
Transgenic expression of the dicotyledonous pattern recognition receptor EFR in rice leads to ligand-dependent activation of defense responses 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/006155v1?rss=1"
</link>
<description><![CDATA[
Plant plasma membrane localized pattern recognition receptors (PRRs) detect extracellular pathogen-associated molecules. PRRs such as Arabidopsis EFR and rice XA21 are taxonomically restricted and are absent from most plant genomes. Here we show that rice plants expressing EFR or the chimeric receptor EFR::XA21, containing the EFR ectodomain and the XA21 intracellular domain, sense both Escherichia coli- and Xanthomonas oryzae pv. oryzae (Xoo)-derived elf18 peptides at sub-nanomolar concentrations. Treatment of EFR and EFR::XA21 rice leaf tissue with elf18 leads to MAP kinase activation, reactive oxygen production and defense gene expression. Although expression of EFR does not lead to robust enhanced resistance to fully virulent Xoo isolates, it does lead to quantitatively enhanced resistance to weakly virulent Xoo isolates. EFR interacts with OsSERK2 and the XA21 binding protein 24 (XB24), two key components of the rice XA21-mediated immune response. Rice-EFR plants silenced for OsSERK2, or overexpressing rice XB24 are compromised in elf18-induced reactive oxygen production and defense gene expression indicating that these proteins are also important for EFR-mediated signaling in transgenic rice. Taken together, our results demonstrate the potential feasibility of enhancing disease resistance in rice and possibly other monocotyledonous crop species by expression of dicotyledonous PRRs. Our results also suggest that Arabidopsis EFR utilizes at least a subset of the known endogenous rice XA21 signaling components.nnAuthor SummaryPlants possess multi-layered immune recognition systems. Early in the infection process, plants use receptor proteins to recognize pathogen molecules. Some of these receptors are present in only in a subset of plant species. Transfer of these taxonomically restricted immune receptors between plant species by genetic engineering is a promising approach for boosting the plant immune system. Here we show the successful transfer of an immune receptor from a species in the mustard family, called EFR, to rice. Rice plants expressing EFR are able to sense the bacterial ligand of EFR and elicit an immune response. We show that the EFR receptor is able to use components of the rice immune signaling pathway for its function. Under laboratory conditions, this leads to an enhanced resistance response to two weakly virulent isolates of an economically important bacterial disease of rice.
]]></description>
<dc:creator>Benjamin Schwessinger</dc:creator>
<dc:creator>Ofir Bahar</dc:creator>
<dc:creator>Thomas Nicolas</dc:creator>
<dc:creator>Nicolas Holton</dc:creator>
<dc:creator>Vladimir Nekrasov</dc:creator>
<dc:creator>Randy Ruan</dc:creator>
<dc:creator>Patrick Canlas</dc:creator>
<dc:creator>Arsalan Daudi</dc:creator>
<dc:creator>Christopher Petzold</dc:creator>
<dc:creator>Vasanth Singan</dc:creator>
<dc:creator>Rita Kuo</dc:creator>
<dc:creator>Mansi Chovatia</dc:creator>
<dc:creator>Chris Daum</dc:creator>
<dc:creator>Joshua Heazlewood</dc:creator>
<dc:creator>Cyril Zipfel</dc:creator>
<dc:creator>Pamela Ronald</dc:creator>
<dc:creator></dc:creator>
<dc:date>2014-06-11</dc:date>
<dc:identifier>doi:10.1101/006155</dc:identifier>
<dc:title><![CDATA[Transgenic expression of the dicotyledonous pattern recognition receptor EFR in rice leads to ligand-dependent activation of defense responses]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2014-06-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/002766v1?rss=1">
<title>
<![CDATA[
A Novel Approach for Multi-Domain and Multi-Gene Family Identification Provides Insights into Evolutionary Dynamics of Disease Resistance Genes in Core Eudicot Plants 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/002766v1?rss=1"
</link>
<description><![CDATA[
Recent advances in DNA sequencing techniques resulted in more than forty sequenced plant genomes representing a diverse set of taxa of agricultural, energy, medicinal and ecological importance. However, gene family curation is often only inferred from DNA sequence homology and lacks insights into evolutionary processes contributing to gene family dynamics. In a comparative genomics framework, we integrated multiple lines of evidence provided by gene synteny, sequence homology and protein-based Hidden Markov Modelling to extract homologous super-clusters composed of multi-domain resistance (R)-proteins of the NB-LRR type (for NUCLEOTIDE BINDING/LEUCINE-RICH REPEATS), that are involved in plant innate immunity. To assess the diversity of R-proteins within and between species, we screened twelve eudicot plant genomes including six major crops and found a total of 2,363 NB-LRR genes. Our curated R-proteins set shows a 50% average for tandem duplicates and a 22% fraction of gene copies retained from ancient polyploidy events (ohnologs). We provide evidence for strong positive selection acting on all identified genes and show significant differences in molecular evolution rates (Ka/Ks-ratio) among tandem- (mean = 1.59), ohnolog (mean = 1.36) and singleton (mean = 1.22) R-gene duplicates. To foster the process of gene-edited plant breeding, we report species-specific presence/absence of all 140 NB-LRR genes present in the model plant Arabidopsis and describe four distinct clusters of NB-LRR "gatekeeper" loci sharing syntelogs across all analyzed genomes. In summary, we designed and implemented an easy-to-follow computational framework for super-gene family identification, and provide the most curated set of NB-LRR genes whose genetic versatility among twelve lineages can underpin crop improvement.
]]></description>
<dc:creator>Johannes A. Hofberger</dc:creator>
<dc:creator>Beifei Zhou</dc:creator>
<dc:creator>Haibao Tang</dc:creator>
<dc:creator>Jonathan DG Jones</dc:creator>
<dc:creator>M. Eric Schranz</dc:creator>
<dc:creator></dc:creator>
<dc:date>2014-02-17</dc:date>
<dc:identifier>doi:10.1101/002766</dc:identifier>
<dc:title><![CDATA[A Novel Approach for Multi-Domain and Multi-Gene Family Identification Provides Insights into Evolutionary Dynamics of Disease Resistance Genes in Core Eudicot Plants]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2014-02-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/171223v1?rss=1">
<title>
<![CDATA[
Lessons in effector and NLR biology of plant-microbe systems 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/171223v1?rss=1"
</link>
<description><![CDATA[
A diversity of plant-associated organisms secrete effectors--proteins and metabolites that modulate plant physiology to favor host infection and colonization. However, effectors can also activate plant immune receptors, notably nucleotide-binding domain and leucine-rich repeat-containing (NLR) proteins, enabling plants to fight off invading organisms. This interplay between effectors, their host targets, and the matching immune receptors is shaped by intricate molecular mechanisms and exceptionally dynamic coevolution. In this article, we focus on three effectors, AVR-Pik, AVR-Pia, and AVR-Pii, from the rice blast fungus Magnaporthe oryzae (syn. Pyricularia oryzae), and their corresponding rice NLR immune receptors, Pik, Pia, and Pii, to highlight general concepts of plant-microbe interactions. We draw 12 lessons in effector and NLR biology that have emerged from studying these three little effectors and are broadly applicable to other plant-microbe systems.
]]></description>
<dc:creator>Bialas, A.</dc:creator>
<dc:creator>Zess, E. K.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Franceschetti, M.</dc:creator>
<dc:creator>Pennington, H. G.</dc:creator>
<dc:creator>Yoshida, K.</dc:creator>
<dc:creator>Upson, J. L.</dc:creator>
<dc:creator>Chanclud, E.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Varden, F. A.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Belhaj, K.</dc:creator>
<dc:creator>Fujisaki, K.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2017-08-02</dc:date>
<dc:identifier>doi:10.1101/171223</dc:identifier>
<dc:title><![CDATA[Lessons in effector and NLR biology of plant-microbe systems]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-08-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/171868v1?rss=1">
<title>
<![CDATA[
Heterologous expression of the immune receptor EFR in Medicago truncatula reduces pathogenic infection, but not rhizobial symbiosis 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/171868v1?rss=1"
</link>
<description><![CDATA[
Interfamily transfer of plant pattern recognition receptors (PRRs) represents a promising biotechnological approach to engineer broad-spectrum, and potentially durable, disease resistance in crops. It is however unclear whether new recognition specificities to given pathogen-associated molecular patterns (PAMPs) affect the interaction of the recipient plant with beneficial microbes. To test this in a direct reductionist approach, we transferred the Brassicaceae-specific PRR ELONGATION FACTOR-THERMO UNSTABLE RECEPTOR (EFR) from Arabidopsis thaliana to the legume Medicago truncatula, conferring recognition of the bacterial EF-Tu protein. Constitutive EFR expression led to EFR accumulation and activation of immune responses upon treatment with the EF-Tu-derived elf18 peptide in leaves and roots. The interaction of M. truncatula with the bacterial symbiont Sinorhizobium meliloti is characterized by the formation of root nodules that fix atmospheric nitrogen. Although nodule numbers were slightly reduced at an early stage of the infection in EFR-Medicago when compared to control lines, nodulation was similar in all lines at later stages. Furthermore, nodule colonization by rhizobia, and nitrogen fixation were not compromised by EFR expression. Importantly, the M. truncatula lines expressing EFR were substantially more resistant to the root bacterial pathogen Ralstonia solanacearum. Our data suggest that the transfer of EFR to M. truncatula does not impede root nodule symbiosis, but has a positive impact on disease resistance against a bacterial pathogen. In addition, our results indicate that Rhizobium can either avoid PAMP recognition during the infection process, or is able to actively suppress immune signaling.nnSignificance StatementCrop engineering helps reducing the economic and environmental costs of plant disease. The genetic transfer of immune receptors across plant species is a promising biotechnological approach to increase disease resistance. Surface-localized pattern-recognition receptors (PRRs), which detect conserved characteristic microbial features, are functional in heterologous taxonomically-diverse plant species, and confer broad-spectrum disease resistance. It was unclear whether PRR transfer negatively impacts the association of the recipient plants with symbiotic microbes. Here, we show that a legume engineered with a novel PRR recognizing a conserved bacterial protein becomes more resistant to an important bacterial pathogen without significant impact on nitrogen-fixing symbiosis with rhizobia. This finding is of particular relevance as attempts to transfer this important symbiosis into non-legume plants are ongoing.
]]></description>
<dc:creator>Pfeilmeier, S.</dc:creator>
<dc:creator>George, J.</dc:creator>
<dc:creator>Morel, A.</dc:creator>
<dc:creator>Roy, S.</dc:creator>
<dc:creator>Smoker, M.</dc:creator>
<dc:creator>Stansfeld, L.</dc:creator>
<dc:creator>Downie, A.</dc:creator>
<dc:creator>Peeters, N.</dc:creator>
<dc:creator>Malone, J.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2017-08-02</dc:date>
<dc:identifier>doi:10.1101/171868</dc:identifier>
<dc:title><![CDATA[Heterologous expression of the immune receptor EFR in Medicago truncatula reduces pathogenic infection, but not rhizobial symbiosis]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-08-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/205765v1?rss=1">
<title>
<![CDATA[
The plant calcium-dependent protein kinase CPK3 phosphorylates REM1.3 to restrict viral infection 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/205765v1?rss=1"
</link>
<description><![CDATA[
Plants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 proteins and subsequently trigger the activation of a membrane-bound calcium-dependent kinase. We show that the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3-interacts with group 1 REMORINs in vivo, phosphorylates the intrinsically disordered N-terminal domain of the Group 1 REMORIN REM1.3, and restricts PVX cell-to-cell movement. REM1.3-s phospho-status defines its plasma membrane nanodomain organization and is crucial for REM1.3-dependent restriction of PVX cell-to-cell movement by regulation of callose deposition at plasmodesmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses.
]]></description>
<dc:creator>Perraki, A.</dc:creator>
<dc:creator>Gronnier, J.</dc:creator>
<dc:creator>Gouguet, P.</dc:creator>
<dc:creator>Boudsocq, M.</dc:creator>
<dc:creator>Deroubaix, A.-F.</dc:creator>
<dc:creator>Simon, V.</dc:creator>
<dc:creator>German-Retana, S.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Bayer, E.</dc:creator>
<dc:creator>Mongrand, S.</dc:creator>
<dc:creator>Germain, V.</dc:creator>
<dc:date>2017-10-19</dc:date>
<dc:identifier>doi:10.1101/205765</dc:identifier>
<dc:title><![CDATA[The plant calcium-dependent protein kinase CPK3 phosphorylates REM1.3 to restrict viral infection]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-10-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/217646v1?rss=1">
<title>
<![CDATA[
Phytophthora methylomes modulated by expanded 6mA methyltransferases are associated with adaptive genome regions 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/217646v1?rss=1"
</link>
<description><![CDATA[
Filamentous plant pathogen genomes often display a bipartite architecture with gene sparse, repeat-rich compartments serving as a cradle for adaptive evolution. However, the extent to which this "two-speed" genome architecture is associated with genome-wide epigenetic modifications is unknown. Here, we show that the oomycete plant pathogens Phytophthora infestans and Phytophthora sojae possess functional adenine N6- methylation (6mA) methyltransferases that modulate patterns of 6mA marks across the genome. In contrast, 5-methylcytosine (5mC) could not be detected in the two Phytophthora species. Methylated DNA IP Sequencing (MeDIP-seq) of each species revealed that 6mA is depleted around the transcriptional starting sites (TSS) and is associated with low expressed genes, particularly transposable elements. Remarkably, genes occupying the gene-sparse regions have higher levels of 6mA compared to the remainder of both genomes, possibly implicating the methylome in adaptive evolution of Phytophthora. Among three putative adenine methyltransferases, DAMT1 and DAMT3 displayed robust enzymatic activities. Surprisingly, single knockouts of each of the 6mA methyltransferases in P. sojae significantly reduced in vivo 6mA levels, indicating that the three enzymes are not fully redundant. MeDIP-seq of the damt3 mutant revealed uneven patterns of 6mA methylation across genes, suggesting that PsDAMT3 may have a preference for gene body methylation after the TSS. Our findings provide evidence that 6mA modification is an epigenetic mark of Phytophthora genomes and that complex patterns of 6mA methylation by the expanded 6mA methyltransferases may be associated with adaptive evolution in these important plant pathogens.
]]></description>
<dc:creator>Chen, H.</dc:creator>
<dc:creator>Shu, H.</dc:creator>
<dc:creator>Wang, L.</dc:creator>
<dc:creator>Zhang, F.</dc:creator>
<dc:creator>Li, X.</dc:creator>
<dc:creator>Ochola, S.</dc:creator>
<dc:creator>Mao, F.</dc:creator>
<dc:creator>Ma, H.</dc:creator>
<dc:creator>Ye, W.</dc:creator>
<dc:creator>Gu, T.</dc:creator>
<dc:creator>Jiang, L.</dc:creator>
<dc:creator>Wu, Y.</dc:creator>
<dc:creator>Wang, Y.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Dong, S.</dc:creator>
<dc:date>2017-11-11</dc:date>
<dc:identifier>doi:10.1101/217646</dc:identifier>
<dc:title><![CDATA[Phytophthora methylomes modulated by expanded 6mA methyltransferases are associated with adaptive genome regions]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-11-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/239400v1?rss=1">
<title>
<![CDATA[
An unconventional NOI/RIN4 domain of a rice NLR protein binds host EXO70 protein to confer fungal immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/239400v1?rss=1"
</link>
<description><![CDATA[
As much as 10% of plant immune receptors from the nucleotide-binding domain leucine-rich repeat (NLR) family carry integrated domains (IDs) that can directly bind pathogen effectors. However, it remains unclear whether direct binding to effectors is a universal feature of ID-containing NLRs given that only a few NLR-IDs have been functionally characterized. Here we show that the rice (Oryza sativa) sensor NLR-ID Pii2 confers resistance to strains of the rice blast fungus Magnaporthe oryzae that carry the effector AVR-Pii without directly binding this protein. First, we show that AVR-Pii binds the exocyst subunit OsExo70F2 in rice (Oryza sativa) to dissociate preformed complexes of OsExo70F2 with host RPM1 INTERACTING PROTEIN4 (RIN4) at the conserved NOI motif, facilitating a possible virulence function. Second, we show that in its resting state, Pii2 binds OsExo70F2 and OsExo70F3, essential components of Pii-mediated resistance, through its integrated NOI domain. Remarkably, AVR-Pii binding to OsExo70F2/F3 leads to dissociation of the Pii2-OsExo70F2 and Pii2-OsExo70F3 complexes, destabilization of Pii2, and activation of immunity. These findings support a novel conceptual model in which an NLR-ID monitors alterations of tethered host proteins targeted by pathogen effectors, providing insight into pathogen recognition mechanisms.

Significance statementPlant diseases diminish crop yields by over 20% each year, and deploying resistant crops is the most effective way to combat them. Nucleotide-binding domain leucine-rich repeat (NLR)-type receptors are the major player in plant resistance against pathogens, with a subset of NLRs containing unconventional domains called integrated domains (ID) derived from host proteins. Previous studies suggest that pathogen avirulence (AVR) effectors directly bind or modify NLR-IDs before they are recognized by the host. Here, we reveal that the rice NLR-ID receptor Pii2 indirectly recognizes AVR-Pii when the effector dissociates Pii2 from the host Exo70 proteins tethered to Pii2. We propose a new model of how NLRs can recognize pathogens, expanding our understanding of plant immunity.
]]></description>
<dc:creator>Fujisaki, K.</dc:creator>
<dc:creator>Abe, Y.</dc:creator>
<dc:creator>Kanzaki, E.</dc:creator>
<dc:creator>Ito, K.</dc:creator>
<dc:creator>Utsushi, H.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>Białas, A.</dc:creator>
<dc:creator>Banfield, M.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:date>2017-12-24</dc:date>
<dc:identifier>doi:10.1101/239400</dc:identifier>
<dc:title><![CDATA[An unconventional NOI/RIN4 domain of a rice NLR protein binds host EXO70 protein to confer fungal immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-12-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/239541v1?rss=1">
<title>
<![CDATA[
An ancient integration in a plant NLR is maintained as a trans-species polymorphism 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/239541v1?rss=1"
</link>
<description><![CDATA[
Main text Main text Methods Author contributions Competing interests References Plant immune receptors are under constant selective pressure to maintain resistance to plant pathogens. Nucleotide-binding leucine-rich repeat (NLR) proteins are one class of cytoplasmic immune receptors whose genes commonly show signatures of adaptive evolution1,2. While it is known that balancing selection contributes to maintaining high intraspecific allelic diversity, the evolutionary mechanism that influences the transmission of alleles during speciation remains unclear. The barley Mla locus has over 30 described alleles conferring isolate-specific resistance to barley powdery mildew and contains three NLR families (RGH1, RGH2, and RGH3)3. We discov ...
]]></description>
<dc:creator>Brabham, H. J.</dc:creator>
<dc:creator>Hernandez-Pinzon, I.</dc:creator>
<dc:creator>Holden, S.</dc:creator>
<dc:creator>Lorang, J.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:date>2017-12-25</dc:date>
<dc:identifier>doi:10.1101/239541</dc:identifier>
<dc:title><![CDATA[An ancient integration in a plant NLR is maintained as a trans-species polymorphism]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2017-12-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/248146v1?rss=1">
<title>
<![CDATA[
Resistance gene discovery and cloning by sequence capture and association genetics 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/248146v1?rss=1"
</link>
<description><![CDATA[
Genetic resistance is the most economic and environmentally sustainable approach for crop disease protection. Disease resistance (R) genes from wild relatives are a valuable resource for breeding resistant crops. However, introgression of R genes into crops is a lengthy process often associated with co-integration of deleterious linked genes1, 2 and pathogens can rapidly evolve to overcome R genes when deployed singly3. Introducing multiple cloned R genes into crops as a stack would avoid linkage drag and delay emergence of resistance-breaking pathogen races4. However, current R gene cloning methods require segregating or mutant progenies5-10, which are difficult to generate for many wild relatives due to poor agronomic traits. We exploited natural pan-genome variation in a wild diploid wheat by combining association genetics with R gene enrichment sequencing (AgRenSeq) to clone four stem rust resistance genes in <6 months. RenSeq combined with diversity panels is therefore a major advance in isolating R genes for engineering broad-spectrum resistance in crops.
]]></description>
<dc:creator>Arora, S.</dc:creator>
<dc:creator>Steuernagel, B.</dc:creator>
<dc:creator>Chandramohan, S.</dc:creator>
<dc:creator>Long, Y.</dc:creator>
<dc:creator>Matny, O.</dc:creator>
<dc:creator>Johnson, R.</dc:creator>
<dc:creator>Enk, J.</dc:creator>
<dc:creator>Periyannan, S.</dc:creator>
<dc:creator>Hatta, M. A. M.</dc:creator>
<dc:creator>Athiyannan, N.</dc:creator>
<dc:creator>Cheema, J.</dc:creator>
<dc:creator>Yu, G.</dc:creator>
<dc:creator>Kangara, N.</dc:creator>
<dc:creator>Ghosh, S.</dc:creator>
<dc:creator>Szabo, L. J.</dc:creator>
<dc:creator>Poland, J.</dc:creator>
<dc:creator>Bariana, H.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:creator>Bentley, A. R.</dc:creator>
<dc:creator>Ayliffe, M.</dc:creator>
<dc:creator>Olson, E.</dc:creator>
<dc:creator>Xu, S. S.</dc:creator>
<dc:creator>Steffenson, B. J.</dc:creator>
<dc:creator>Lagudah, E.</dc:creator>
<dc:creator>Wulff, B. B. H.</dc:creator>
<dc:date>2018-01-15</dc:date>
<dc:identifier>doi:10.1101/248146</dc:identifier>
<dc:title><![CDATA[Resistance gene discovery and cloning by sequence capture and association genetics]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-01-15</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/254755v1?rss=1">
<title>
<![CDATA[
The coming of age of EvoMPMI: evolutionary molecular plant-microbe interactions across multiple timescales 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/254755v1?rss=1"
</link>
<description><![CDATA[
Plant-microbe interactions are great model systems to study co-evolutionary dynamics across multiple timescales, ranging from multimillion year macroevolution to extremely rapid evolutionary adaptations. However, mechanistic research on plant-microbe interactions has often been conducted with little consideration of the insights that can be gained from evolutionary concepts and methods. Conversely, evolutionary research has rarely integrated the diverse range of molecular mechanisms and models that continue to emerge from the molecular plant-microbe interactions field. These trends are changing. In recent years, the incipient field of evolutionary molecular plant-microbe interactions (EvoMPMI) has emerged to bridge the gap between mechanistic molecular research and evolutionary approaches. Here, we report on recent advances in EvoMPMI. In particular, we highlight new systems to study microbe interactions with early diverging land plants, and new findings from studies of adaptive evolution in pathogens and plants. By linking mechanistic and evolutionary research, EvoMPMI promises to add a new dimension to our understanding of plant-microbe interactions.
]]></description>
<dc:creator>Upson, J. L.</dc:creator>
<dc:creator>Zess, E. K.</dc:creator>
<dc:creator>Bialas, A.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2018-01-28</dc:date>
<dc:identifier>doi:10.1101/254755</dc:identifier>
<dc:title><![CDATA[The coming of age of EvoMPMI: evolutionary molecular plant-microbe interactions across multiple timescales]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-01-28</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/351056v1?rss=1">
<title>
<![CDATA[
TTL proteins scaffold brassinosteroid signaling components at the plasma membrane to optimize signal transduction in plant cells 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/351056v1?rss=1"
</link>
<description><![CDATA[
Brassinosteroids (BRs) form a group of steroidal hormones essential for plant growth, development and stress responses. Here, we report that plant-specific TETRATRICOPEPTIDE THIOREDOXIN-LIKE (TTL) proteins are positive regulators of BR signaling functioning as scaffold for BR signaling components in Arabidopsis. TTL3 forms a complex with all core components involved in BR signaling, including the receptor kinase BRASSINOSTEROID INSENSITIVE1 (BRI1), the transcription factor BRASSINAZOLE RESISTANT1 (BZR1) and the phosphatase BRI1-SUPPRESSOR1 (BSU1), but excluding the co-receptor BAK1. TTL3 is mainly localized in the cytoplasm, but BR treatment increases its localization at the plasma membrane, where it strengthens the association with BR signaling components. Consistent with a role in BR signaling, mutations in TTL3 and related TTL1 and TTL4 genes cause reduced BR responsiveness. We propose a mechanistic model for BR signaling, in which cytoplasmic/nuclear BR components bound to TTL proteins are recruited to the plasma membrane upon BR perception, which in turn allows the assembly of a BR signaling complex, leading to the de-phosphorylation and nuclear accumulation of the transcription factors BZR1 and BES1.
]]></description>
<dc:creator>Amorim-Silva, V.</dc:creator>
<dc:creator>Garcia-Moreno, A.</dc:creator>
<dc:creator>Castillo, A. G.</dc:creator>
<dc:creator>Lakhssassi, N.</dc:creator>
<dc:creator>Perez-Sancho, J.</dc:creator>
<dc:creator>Li, Y.</dc:creator>
<dc:creator>Esteban del Valle, A.</dc:creator>
<dc:creator>Pose, D.</dc:creator>
<dc:creator>Perez-Rodriguez, J.</dc:creator>
<dc:creator>Lin, J.</dc:creator>
<dc:creator>Valpuesta, V.</dc:creator>
<dc:creator>Borsani, O.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Macho, A. P.</dc:creator>
<dc:creator>Botella, M. A.</dc:creator>
<dc:date>2018-06-20</dc:date>
<dc:identifier>doi:10.1101/351056</dc:identifier>
<dc:title><![CDATA[TTL proteins scaffold brassinosteroid signaling components at the plasma membrane to optimize signal transduction in plant cells]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-06-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/345215v1?rss=1">
<title>
<![CDATA[
The MoT3 assay does not distinguish between Magnaporthe oryzae wheat and rice blast isolates from Bangladesh 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/345215v1?rss=1"
</link>
<description><![CDATA[
The blast fungus Magnaporthe oryzae is comprised of lineages that exhibit varying degrees of specificity on about 50 grass hosts, including rice, wheat and barley. Reliable diagnostic tools are essential given that the pathogen has a propensity to jump to new hosts and spread to new geographic regions. Of particular concern is wheat blast, which has suddenly appeared in Bangladesh in 2016 before spreading to neighboring India. In these Asian countries, wheat blast strains are now co-occurring with the destructive rice blast pathogen raising the possibility of genetic exchange between these destructive pathogens. We assessed the recently described MoT3 diagnostic assay and found that it did not distinguish between wheat and rice blast isolates from Bangladesh. The assay is based on primers matching the WB12 sequence corresponding to a fragment of the M. oryzae MGG_02337 gene annotated as a short chain dehydrogenase. These primers could not reliably distinguish between wheat and rice blast isolates from Bangladesh based on DNA amplification experiments performed in separate laboratories in Bangladesh and in the UK. In addition, comparative genomics of the WB12 sequence revealed a complex underlying genetic structure with related sequences across M. oryzae strains and in both rice and wheat blast isolates. We, therefore, caution against the indiscriminate use of this assay to identify wheat blast.
]]></description>
<dc:creator>Gupta, D. R.</dc:creator>
<dc:creator>Reyes Avila, C. S.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Soanes, D. M.</dc:creator>
<dc:creator>Ryder, L. S.</dc:creator>
<dc:creator>Croll, D.</dc:creator>
<dc:creator>Bhattacharjee, P.</dc:creator>
<dc:creator>Hossain, M. S.</dc:creator>
<dc:creator>Mahmud, N. U.</dc:creator>
<dc:creator>Mehbub, M. S.</dc:creator>
<dc:creator>Surovy, M. Z.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Islam, M. T.</dc:creator>
<dc:date>2018-06-14</dc:date>
<dc:identifier>doi:10.1101/345215</dc:identifier>
<dc:title><![CDATA[The MoT3 assay does not distinguish between Magnaporthe oryzae wheat and rice blast isolates from Bangladesh]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-06-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/339424v1?rss=1">
<title>
<![CDATA[
Physical and transcriptional organisation of the bread wheat intracellular immune receptor repertoire 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/339424v1?rss=1"
</link>
<description><![CDATA[
Disease resistance genes encoding intracellular immune receptors of the nucleotide-binding and leucine-rich repeat (NLR) class of proteins detect pathogens by the presence of pathogen effectors. Plant genomes typically contain hundreds of NLR encoding genes. The availability of the hexaploid wheat cultivar Chinese Spring reference genome now allows a detailed study of its NLR complement. However, low NLR expression as well as high intra-family sequence homology hinders their accurate gene annotation. Here we developed NLR-Annotator for in silico NLR identification independent of transcript support. Although developed for wheat, we demonstrate the universal applicability of NLR-Annotator across diverse plant taxa. Applying our tool to wheat and combining it with a transcript-validated subset of genes from the reference gene annotation, we characterized the structure, phylogeny and expression profile of the NLR gene family. We detected 3,400 full-length NLR loci of which 1,540 were confirmed as complete genes. NLRs with integrated domains mostly group in specific sub-clades. Members of another subclade predominantly locate in close physical proximity to NLRs carrying integrated domains suggesting a paired helper-function. Most NLRs (88%) display low basal expression (in the lower 10 percentile of transcripts), which may be tissue-specific and/or induced by biotic stress. As a case study for applying our tool to the positional cloning of resistance genes, we estimated the number of NLR genes within the intervals of mapped rust resistance genes. Our study will support the identification of functional resistance genes in wheat to accelerate the breeding and engineering of disease resistant varieties.
]]></description>
<dc:creator>Steuernagel, B.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Krattinger, S. G.</dc:creator>
<dc:creator>Ramirez-Gonzalez, R. H.</dc:creator>
<dc:creator>Schoonbeek, H.-j.</dc:creator>
<dc:creator>Yu, G.</dc:creator>
<dc:creator>Baggs, E.</dc:creator>
<dc:creator>Witek, A.</dc:creator>
<dc:creator>Yadav, I.</dc:creator>
<dc:creator>Krasileva, K. V.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:creator>Uauy, C.</dc:creator>
<dc:creator>Keller, B.</dc:creator>
<dc:creator>Ridout, C. J.</dc:creator>
<dc:creator>The International Wheat Genome Sequencing Consortium,</dc:creator>
<dc:creator>Wulff, B.</dc:creator>
<dc:date>2018-06-05</dc:date>
<dc:identifier>doi:10.1101/339424</dc:identifier>
<dc:title><![CDATA[Physical and transcriptional organisation of the bread wheat intracellular immune receptor repertoire]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-06-05</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/291427v1?rss=1">
<title>
<![CDATA[
A fungal ribonuclease-like effector protein inhibits plant host ribosomal RNA degradation 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/291427v1?rss=1"
</link>
<description><![CDATA[
The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. Proteins with a predicted ribonuclease (RNase)-like fold (termed RALPHs) comprise the largest set of secreted effector candidates within the B. graminis f. sp. hordei genome. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in monocotyledenous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with five host proteins: two translation elongation factors (eEF1 and eEF1{gamma}), two pathogenesis-related proteins (PR5 and PR10) and a glutathione-S-transferase. We present the first crystal structure of a RALPH, CSEP0064/BEC1054, demonstrating it has an RNase-like fold. The protein interacts with total RNA and weakly with DNA. Methyl jasmonate levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose that CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating proteins that would otherwise lead to host cell death, an unviable interaction and demise of the fungus.
]]></description>
<dc:creator>Spanu, P. D.</dc:creator>
<dc:creator>Pennington, H. G.</dc:creator>
<dc:creator>Jones, R.</dc:creator>
<dc:creator>Kwon, S.</dc:creator>
<dc:creator>Bonciani, G.</dc:creator>
<dc:creator>Thieron, H.</dc:creator>
<dc:creator>Chandler, T.</dc:creator>
<dc:creator>Luong, P.</dc:creator>
<dc:creator>Morgan, S.</dc:creator>
<dc:creator>Przydacz, M.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Bowden, S.</dc:creator>
<dc:creator>Craze, M.</dc:creator>
<dc:creator>Wallington, E.</dc:creator>
<dc:creator>Garnett, J.</dc:creator>
<dc:creator>Kwaitaal, M.</dc:creator>
<dc:creator>Panstruga, R.</dc:creator>
<dc:creator>Cota, E.</dc:creator>
<dc:date>2018-03-29</dc:date>
<dc:identifier>doi:10.1101/291427</dc:identifier>
<dc:title><![CDATA[A fungal ribonuclease-like effector protein inhibits plant host ribosomal RNA degradation]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-03-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/281568v1?rss=1">
<title>
<![CDATA[
Detection of race-specific resistance against Puccinia coronata f. sp. avenae in Brachypodium species 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/281568v1?rss=1"
</link>
<description><![CDATA[
Oat crown rust caused by Puccinia coronata f. sp. avenae is the most destructive foliar disease of cultivated oat. Characterization of genetic factors controlling resistance responses to Puccinia coronata f. sp. avenae in non-host species could provide new resources for developing disease protection strategies in oat. We examined symptom development and fungal colonization levels of a collection of Brachypodium distachyon and B. hybridum accessions infected with three North American P. coronata f. sp. avenae isolates. Our results demonstrated that colonization phenotypes are dependent on both host and pathogen genotypes, indicating a role for race-specific responses in these interactions. These responses were independent of the accumulation of reactive oxygen species. Expression analysis of several defense-related genes suggested that salicylic acid and ethylene-mediated signaling, but not jasmonic acid are components of resistance reaction to P. coronata f. sp. avenae. Our findings provide the basis to conduct a genetic inheritance study to examine if effector-triggered immunity contributes to non-host resistance to P. coronata f. sp. avenae in Brachypodium species.
]]></description>
<dc:creator>Omidvar, V.</dc:creator>
<dc:creator>Dugyala, S.</dc:creator>
<dc:creator>Li, F.</dc:creator>
<dc:creator>Rottschaefer, S.</dc:creator>
<dc:creator>Miller, M.</dc:creator>
<dc:creator>Ayliffe, M.</dc:creator>
<dc:creator>Moscou, M.</dc:creator>
<dc:creator>Kianian, S.</dc:creator>
<dc:creator>Figueroa, M.</dc:creator>
<dc:date>2018-03-13</dc:date>
<dc:identifier>doi:10.1101/281568</dc:identifier>
<dc:title><![CDATA[Detection of race-specific resistance against Puccinia coronata f. sp. avenae in Brachypodium species]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-03-13</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/365098v1?rss=1">
<title>
<![CDATA[
DeepStomata: Facial Recognition Technology for Automated Stomatal Aperture Measurement 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/365098v1?rss=1"
</link>
<description><![CDATA[
Stomata are an attractive model for studying the physiological responses of plants to various environmental stimuli1-3. Of the morphological parameters that represent the degree of stomatal opening, the length of the minor axis of the stomatal pore (the stomatal aperture) has been most commonly used to dissect the molecular basis of its regulation. Measuring stomatal apertures is time consuming and labour intensive, preventing their use in large-scale studies. Here, we completely automated this process by developing a program called DeepStomata, which combines stomatal region detection and pore isolation by image segmentation. The former, which comprises histograms of oriented gradients (HOG)-based stomatal detection and the convolutional neural network (CNN)-based classification of open/closed-state stomata, acts as an efficient conditional branch in the workflow to selectively quantify the pores of open stomata. An analysis of batches of images showed that the accuracy of our automated aperture measurements was equivalent to that of manual measurements, however had higher sensitivity (i,e., lower false negative rate) and the process speed was at least 80 times faster. The outstanding performance of our proposed method for automating a laborious and repetitive task will allow researchers to focus on deciphering complex phenomena.
]]></description>
<dc:creator>Toda, Y.</dc:creator>
<dc:creator>Toh, S.</dc:creator>
<dc:creator>Bourdais, G.</dc:creator>
<dc:creator>Robatzek, S.</dc:creator>
<dc:creator>Maclean, D.</dc:creator>
<dc:creator>Kinoshita, T.</dc:creator>
<dc:date>2018-07-09</dc:date>
<dc:identifier>doi:10.1101/365098</dc:identifier>
<dc:title><![CDATA[DeepStomata: Facial Recognition Technology for Automated Stomatal Aperture Measurement]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-07-09</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/419952v1?rss=1">
<title>
<![CDATA[
Optimization of T-DNA architecture for Cas9-mediated mutagenesis in Arabidopsis 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/419952v1?rss=1"
</link>
<description><![CDATA[
Bacterial CRISPR systems have been widely adopted to create operator-specified site-specific nucleases. Such nuclease action commonly results in loss-of-function alleles, facilitating functional analysis of genes and gene families We conducted a systematic comparison of components and T-DNA architectures for CRISPR-mediated gene editing in Arabidopsis, testing multiple promoters, terminators, sgRNA backbones and Cas9 alleles. We identified a T-DNA architecture that usually results in stable (i.e. homozygous) mutations in the first generation after transformation. Notably, the transcription of sgRNA and Cas9 in head-to-head divergent orientation usually resulted in highly active lines. Our Arabidopsis data may prove useful for optimization of CRISPR methods in other plants.
]]></description>
<dc:creator>Castel, B.</dc:creator>
<dc:creator>Tomlinson, L.</dc:creator>
<dc:creator>Locci, F.</dc:creator>
<dc:creator>Yang, Y.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:date>2018-09-17</dc:date>
<dc:identifier>doi:10.1101/419952</dc:identifier>
<dc:title><![CDATA[Optimization of T-DNA architecture for Cas9-mediated mutagenesis in Arabidopsis]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-09-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/453563v1?rss=1">
<title>
<![CDATA[
N-terminal β-strand underpins biochemical specialization of an ATG8 isoform 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/453563v1?rss=1"
</link>
<description><![CDATA[
ATG8 is a highly-conserved ubiquitin-like protein that modulates autophagy pathways by binding autophagic membranes and numerous proteins, including cargo receptors and core autophagy components. Throughout plant evolution, ATG8 has expanded from a single protein in algae to multiple isoforms in higher plants. However, the degree to which ATG8 isoforms have functionally specialized to bind distinct proteins remains unclear. Here, we describe a comprehensive protein-protein interaction resource, obtained using in planta immunoprecipitation followed by mass spectrometry, to define the potato ATG8 interactome. We discovered that ATG8 isoforms bind distinct sets of plant proteins with varying degrees of overlap. This prompted us to define the biochemical basis of ATG8 specialization by comparing two potato ATG8 isoforms using both in vivo protein interaction assays and in vitro quantitative binding affinity analyses. These experiments revealed that the N-terminal {beta}-strand--and, in particular, a single amino acid polymorphism--underpins binding specificity to the substrate PexRD54 by shaping the hydrophobic pocket that accommodates this proteins ATG8 interacting motif. Additional proteomics experiments indicated that the N-terminal {beta}-strand shapes the ATG8 interactor profiles, defining interaction specificity with about 80 plant proteins. Our findings are consistent with the view that ATG8 isoforms comprise a layer of specificity in the regulation of selective autophagy pathways in plants.
]]></description>
<dc:creator>Zess, E. K.</dc:creator>
<dc:creator>Jensen, C.</dc:creator>
<dc:creator>Cruz-Mireles, N.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Imre, R.</dc:creator>
<dc:creator>Roitinger, E.</dc:creator>
<dc:creator>Hughes, R.</dc:creator>
<dc:creator>Belhaj, K.</dc:creator>
<dc:creator>Mechtler, K.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Bozkurt, T.</dc:creator>
<dc:creator>Banfield, M.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Dagdas, Y.</dc:creator>
<dc:date>2018-10-25</dc:date>
<dc:identifier>doi:10.1101/453563</dc:identifier>
<dc:title><![CDATA[N-terminal β-strand underpins biochemical specialization of an ATG8 isoform]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-10-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/428854v1?rss=1">
<title>
<![CDATA[
CrRLK1L receptor-like kinases HERK1 and ANJEA are female determinants of pollen tube reception 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/428854v1?rss=1"
</link>
<description><![CDATA[
Communication between the gametophytes is vital for angiosperm fertilisation. Multiple CrRLK1L-type receptor kinases prevent premature pollen tube burst, while another CrRLK1L protein, FERONIA (FER), is required for pollen tube burst in the female gametophyte. We report here the identification of two additional CrRLK1L homologues, HERCULES RECEPTOR KINASE 1 (HERK1) and ANJEA (ANJ), which act redundantly to promote pollen tube burst at the synergid cells. HERK1 and ANJ localise to the filiform apparatus of the synergid cells in unfertilised ovules, and in herk1 anj mutants a majority of ovules remain unfertilised due to pollen tube overgrowth, together indicating that HERK1 and ANJ act as female determinants for fertilisation. As in fer mutants, the synergid cell-specific, endomembrane protein NORTIA (NTA) is not relocalised after pollen tube reception; however, unlike fer mutants, reactive oxygen species levels are unaffected in herk1 anj double mutants. Both ANJ and HERK1 associate with FER and its proposed co-receptor LORELEI (LRE) in planta. Together, our data indicate that HERK1 and ANJ act with FER to mediate female-male gametophyte interactions during plant fertilisation.
]]></description>
<dc:creator>Galindo-Trigo, S.</dc:creator>
<dc:creator>Blanco-Tourinan, N.</dc:creator>
<dc:creator>DeFalco, T. A.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Gray, J. E.</dc:creator>
<dc:creator>Smith, L. M.</dc:creator>
<dc:date>2018-09-27</dc:date>
<dc:identifier>doi:10.1101/428854</dc:identifier>
<dc:title><![CDATA[CrRLK1L receptor-like kinases HERK1 and ANJEA are female determinants of pollen tube reception]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2018-09-27</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/530675v1?rss=1">
<title>
<![CDATA[
Cross-reactivity of a rice NLR immune receptor to distinct effectors from the blast pathogen leads to partial disease resistance 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/530675v1?rss=1"
</link>
<description><![CDATA[
Unconventional integrated domains in plant intracellular immune receptors (NLRs) can directly bind translocated pathogen effector proteins to initiate an immune response. The rice immune receptor pairs Pik-1/Pik-2 and RGA5/RGA4 both use integrated heavy metal-associated (HMA) domains to bind the Magnaporthe oryzae effectors AVR-Pik and AVR-Pia, respectively. These effectors both belong to the MAX effector family and share a core structural fold, despite being divergent in sequence. How integrated domains maintain specificity of recognition, even for structurally similar effectors, has implications for understanding plant immune receptor evolution and function. Here we show that the rice NLR pair Pikp-1/Pikp-2 triggers an immune response leading to partial disease resistance towards the "mismatched" effector AVR-Pia in planta, and that the Pikp-HMA domain binds AVR-Pia in vitro. The HMA domain from another Pik-1 allele, Pikm, is unable to bind AVR-Pia, and does not trigger a response in plants. The crystal structure of Pikp-HMA bound to AVR-Pia reveals a different binding interface compared to AVR-Pik effectors, suggesting plasticity in integrated domain/effector interactions. This work shows how a single NLR can bait multiple pathogen effectors via an integrated domain, and may enable engineering immune receptors with extended disease resistance profiles.
]]></description>
<dc:creator>Varden, F. A.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>YOSHINO, K.</dc:creator>
<dc:creator>Franceschetti, M.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2019-01-25</dc:date>
<dc:identifier>doi:10.1101/530675</dc:identifier>
<dc:title><![CDATA[Cross-reactivity of a rice NLR immune receptor to distinct effectors from the blast pathogen leads to partial disease resistance]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-01-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/537001v1?rss=1">
<title>
<![CDATA[
The Arabidopsis thaliana pan-NLRome 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/537001v1?rss=1"
</link>
<description><![CDATA[
Disease is both among the most important selection pressures in nature and among the main causes of yield loss in agriculture. In plants, resistance to disease is often conferred by Nucleotide-binding Leucine-rich Repeat (NLR) proteins. These proteins function as intracellular immune receptors that recognize pathogen proteins and their effects on the plant. Consistent with evolutionarily dynamic interactions between plants and pathogens, NLRs are known to be encoded by one of the most variable gene families in plants, but the true extent of intraspecific NLR diversity has been unclear. Here, we define the majority of the Arabidopsis thaliana species-wide "NLRome". From NLR sequence enrichment and long-read sequencing of 65 diverse A. thaliana accessions, we infer that the pan-NLRome saturates with approximately 40 accessions. Despite the high diversity of NLRs, half of the pan-NLRome is present in most accessions. We chart the architectural diversity of NLR proteins, identify novel architectures, and quantify the selective forces that act on specific NLRs, domains, and positions. Our study provides a blueprint for defining the pan-NLRome of plant species.
]]></description>
<dc:creator>Van de Weyer, A.-L.</dc:creator>
<dc:creator>Monteiro, F.</dc:creator>
<dc:creator>Furzer, O. J.</dc:creator>
<dc:creator>Nishimura, M. T.</dc:creator>
<dc:creator>Cevik, V.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:creator>Dangl, J. L.</dc:creator>
<dc:creator>Weigel, D.</dc:creator>
<dc:creator>Bemm, F.</dc:creator>
<dc:date>2019-01-31</dc:date>
<dc:identifier>doi:10.1101/537001</dc:identifier>
<dc:title><![CDATA[The Arabidopsis thaliana pan-NLRome]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-01-31</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/572560v1?rss=1">
<title>
<![CDATA[
Convergent gene loss in aquatic plants predicts new components of plant immunity and drought response 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/572560v1?rss=1"
</link>
<description><![CDATA[
Plant innate immunity relies on NLR receptors that recognize pathogen derived molecules and activate downstream signalling pathways. We analyzed the variation in copy number of NLR genes across flowering plants, and identified a number of species with a low number of NLRs relative to sister species. Two distinct lineages, one monocot (Lentibulariaceae) and one dicot (Alismatales) encapsulate four species with particularly few NLR genes. In these lineages, loss of NLRs coincided with loss of the well-known downstream immune signalling complex (EDS1-PAD4). When we expanded our analysis across the whole proteomes, we were able to identify other characterized immune genes absent only in Lentibulariaceae and Alismatales. Additionally, we identified a small subset of genes with unknown function convergently lost in all four species. We predicted that some of these genes may have a role in plant immunity. Gene expression analyses confirmed that a group of these genes was differentially expressed under pathogen infection. Another subset of these genes was differentially expressed upon drought providing further evidence of a link between the drought and plant immunity.
]]></description>
<dc:creator>Baggs, E. L.</dc:creator>
<dc:creator>Thanki, A. S.</dc:creator>
<dc:creator>O'Grady, R.</dc:creator>
<dc:creator>Schudoma, C.</dc:creator>
<dc:creator>Haerty, W.</dc:creator>
<dc:creator>Krasileva, K. V.</dc:creator>
<dc:date>2019-03-11</dc:date>
<dc:identifier>doi:10.1101/572560</dc:identifier>
<dc:title><![CDATA[Convergent gene loss in aquatic plants predicts new components of plant immunity and drought response]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-03-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/595744v1?rss=1">
<title>
<![CDATA[
Tomato Prf requires NLR helpers NRC2 and NRC3 to confer resistance against the bacterial speck pathogen Pseudomonas syringae pv. tomato 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/595744v1?rss=1"
</link>
<description><![CDATA[
Bacterial speck, caused by the pathogen Pseudomonas syringae pv. tomato, is one of the most common diseases in tomato production. Together with Pto kinase, the NLR (nucleotide-binding domain leucine-rich repeat containing) protein Prf confers resistance against the bacterial speck pathogen by recognizing AvrPto and AvrPtoB, two Type III effector proteins secreted by P. syringae pv. tomato. This Prf/Pto pathway is part of a complex NLR network in solanaceous plants that mediates resistance to diverse pathogens through the helper NLR proteins NRCs (NLR required for cell death). We previously showed that, in Nicotiana benthamiana, the hypersensitive cell death elicited by expression of AvrPto and Pto, which activate immunity through the endogenous Prf ortholog NbPrf, requires functionally redundant NRC2 and NRC3. However, whether tomato (Solanum lycopersicum) Prf (SlPrf) confers resistance to the bacterial speck pathogen through NRC2 and NRC3 has not been determined. In this study, we show that SlPrf requires NRC2 and NRC3 to trigger hypersensitive cell death and disease resistance in both N. benthamiana and tomato. We found that the hypersensitive cell death induced by AvrPtoB/Pto/SlPrf in N. benthamiana is compromised when NRC2 and NRC3 are silenced, indicating that SlPrf is an NRC2/3-dependent NLR. We validated this finding by showing that silencing NRC2 and NRC3 in the bacterial speck resistant tomato  Rio Grande 76R compromised Prf-mediated resistance. These results indicate that the NRC network extends beyond N. benthamiana to solanaceous crops.
]]></description>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2019-04-01</dc:date>
<dc:identifier>doi:10.1101/595744</dc:identifier>
<dc:title><![CDATA[Tomato Prf requires NLR helpers NRC2 and NRC3 to confer resistance against the bacterial speck pathogen Pseudomonas syringae pv. tomato]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-04-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/611152v1?rss=1">
<title>
<![CDATA[
Protein engineering expands the effector recognition profile of a rice NLR immune receptor 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/611152v1?rss=1"
</link>
<description><![CDATA[
Plant NLR receptors detect pathogen effectors and initiate an immune response. Since their discovery, NLRs have been the focus of protein engineering to improve disease resistance. However, this has proven challenging, in part due to their narrow response specificity. Here, we used structure-guided engineering to expand the response profile of the rice NLR Pikp to variants of the rice blast pathogen effector AVR-Pik. A mutation located within an effector binding interface of the integrated Pikp-HMA domain increased the binding affinity for AVR-Pik variants in vitro and in vivo. This translates to an expanded cell death response to AVR-Pik variants previously unrecognized by Pikp in planta. Structures of the engineered Pikp-HMA in complex with AVR-Pik variants revealed the mechanism of expanded recognition. These results provide a proof-of-concept that protein engineering can improve the utility of plant NLR receptors where direct interaction between effectors and NLRs is established, particularly via integrated domains.
]]></description>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Franceschetti, M.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2019-04-16</dc:date>
<dc:identifier>doi:10.1101/611152</dc:identifier>
<dc:title><![CDATA[Protein engineering expands the effector recognition profile of a rice NLR immune receptor]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-04-16</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/611582v1?rss=1">
<title>
<![CDATA[
Chitin perception in plasmodesmata identifies subcellular, context-specific immune signalling in plants 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/611582v1?rss=1"
</link>
<description><![CDATA[
The plasma membrane (PM) that lines plasmodesmata has a distinct protein and lipid composition, underpinning specific regulation of these connections between cells. The plasmodesmal PM can integrate extracellular signals differently from the cellular PM, but it is not known how this specificity is established or how a single stimulus can trigger independent signalling cascades in neighbouring membrane domains. Here we have used the fungal elicitor chitin to investigate signal integration and responses at the plasmodesmal PM. We found that the plasmodesmal PM employs a receptor complex composed of the LysM receptors LYM2 and LYK4 which respectively change their location and interactions in response to chitin. Downstream, signalling is transmitted via a specific phosphorylation signature of an NADPH oxidase and localised callose synthesis that causes plasmodesmata closure. This demonstrates the plasmodesmal PM deploys both plasmodesmata-specific components and differential activation of PM-common components to independently integrate an immune signal.
]]></description>
<dc:creator>Cheval, C.</dc:creator>
<dc:creator>Johnston, M.</dc:creator>
<dc:creator>Samwald, S.</dc:creator>
<dc:creator>Liu, X.</dc:creator>
<dc:creator>Bellandi, A.</dc:creator>
<dc:creator>Breakspear, A.</dc:creator>
<dc:creator>Kadota, Y.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Faulkner, C.</dc:creator>
<dc:date>2019-04-17</dc:date>
<dc:identifier>doi:10.1101/611582</dc:identifier>
<dc:title><![CDATA[Chitin perception in plasmodesmata identifies subcellular, context-specific immune signalling in plants]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-04-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/618926v1?rss=1">
<title>
<![CDATA[
A convolutonal neural network for predicting transcriptional regulators of genes in Arabidopsis transcriptome data reveals classification based on positive regulatory interactions 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/618926v1?rss=1"
</link>
<description><![CDATA[
Gene Regulatory networks that control gene expression are widely studied yet the interactions that make them up are difficult to predict from high throughput data. Deep Learning methods such as convolutional neural networks can perform surprisingly good classifications on a variety of data types and the matrix-like gene expression profiles would seem to be ideal input data for deep learning approaches. In this short study I compiled training sets of expression data using the Arabidopsis AtGenExpress global stress expression data set and known transcription factor-target interactions from the Arabidopsis PLACE database. I built and optimised convolutional neural networks with a best model providing 95 % accuracy of classification on a held-out validation set. Investigation of the activations within this model revealed that classification was based on positive correlation of expression profiles in short sections. This result shows that a convolutional neural network can be used to make classifications and reveal the basis of those calssifications for gene expression data sets, indicating that a convolutional neural network is a useful and interpretable tool for exploratory classification of biological data. The final model is available for download and as a web application.
]]></description>
<dc:creator>MacLean, D.</dc:creator>
<dc:date>2019-04-26</dc:date>
<dc:identifier>doi:10.1101/618926</dc:identifier>
<dc:title><![CDATA[A convolutonal neural network for predicting transcriptional regulators of genes in Arabidopsis transcriptome data reveals classification based on positive regulatory interactions]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-04-26</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/675678v1?rss=1">
<title>
<![CDATA[
Genome assembly and characterization of a complex zfBED-NLR gene-containing disease resistance locus in Carolina Gold Select rice with Nanopore sequencing 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/675678v1?rss=1"
</link>
<description><![CDATA[
BackgroundLong-read sequencing facilitates assembly of complex genomic regions. In plants, loci containing nucleotide-binding, leucine-rich repeat (NLR) disease resistance genes are an important example of such regions. NLR genes make up one of the largest gene families in plants and are often clustered, evolving via duplication, contraction, and transposition. We recently mapped the Xo1 locus for resistance to bacterial blight and bacterial leaf streak, found in the American heirloom rice variety Carolina Gold Select, to a region that in the Nipponbare reference genome is rich in NLR genes.nnResultsToward identification of the Xo1 gene, we combined Nanopore and Illumina reads to generate a high-quality genome assembly for Carolina Gold Select. We identified 529 full or partial NLR genes and discovered, relative to the reference, an expansion of NLR genes at the Xo1 locus. One NLR gene at Xo1 has high sequence similarity to the cloned, functionally similar Xa1 gene. Both harbor an integrated zfBED domain and near-identical, tandem, C-terminal repeats. Across diverse Oryzeae, we identified two sub-clades of such NLR genes, varying in the presence of the zfBED domain and the number of repeats.nnConclusionsWhole genome sequencing combining Nanopore and Illumina reads effectively resolves NLR gene loci, providing context as well as content. Our identification of an Xo1 candidate is an important step toward mechanistic characterization, including the role(s) of the zfBED domain. Further, the Carolina Gold Select genome assembly will facilitate identification and exploitation of other useful traits in this historically important rice variety.
]]></description>
<dc:creator>Read, A. C.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:creator>Zimin, A. V.</dc:creator>
<dc:creator>Pertea, G.</dc:creator>
<dc:creator>Meyer, R. S.</dc:creator>
<dc:creator>Purugganan, M. D.</dc:creator>
<dc:creator>Leach, J. E.</dc:creator>
<dc:creator>Triplett, L. R.</dc:creator>
<dc:creator>Salzberg, S. L.</dc:creator>
<dc:creator>Bogdanove, A. J.</dc:creator>
<dc:date>2019-06-20</dc:date>
<dc:identifier>doi:10.1101/675678</dc:identifier>
<dc:title><![CDATA[Genome assembly and characterization of a complex zfBED-NLR gene-containing disease resistance locus in Carolina Gold Select rice with Nanopore sequencing]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-06-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/679803v1?rss=1">
<title>
<![CDATA[
A receptor for herbivore-associated molecular patterns mediates plant immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/679803v1?rss=1"
</link>
<description><![CDATA[
Plant-herbivore interactions are ubiquitous across nature and drive major agricultural losses. Inducible defense responses triggered through immune recognition aid in host plant protection; however, specific ligand-receptor pairs mediating the initial perception of herbivory remain unknown. Plants in the subtribe Phaseolinae detect herbivore-associated peptides in caterpillar oral secretions and the defined ligands are proteolytic fragments of chloroplastic ATP synthase termed inceptins. Using forward genetic mapping of inceptin-induced responses, we identify a cowpea (Vigna unguiculata) leucine-rich repeat receptor-like protein as an inceptin receptor (INR) sufficient for elicitor-induced responses and enhanced defense against armyworms (Spodoptera exigua). INR defines a receptor by which plants perceive herbivore-associated molecular patterns (HAMPs) and expands the paradigm of surface immune recognition to attack with mandibles.nnOne Sentence SummaryA plant cell surface receptor directly perceives peptides associated with caterpillar herbivory.
]]></description>
<dc:creator>Steinbrenner, A. D.</dc:creator>
<dc:creator>Munoz-Amatriain, M.</dc:creator>
<dc:creator>Venegas, J. M. A.</dc:creator>
<dc:creator>Lo, S.</dc:creator>
<dc:creator>Shi, D.</dc:creator>
<dc:creator>Holton, N.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Abagyan, R.</dc:creator>
<dc:creator>Huffaker, A.</dc:creator>
<dc:creator>Close, T. J.</dc:creator>
<dc:creator>Schmelz, E. A.</dc:creator>
<dc:date>2019-06-22</dc:date>
<dc:identifier>doi:10.1101/679803</dc:identifier>
<dc:title><![CDATA[A receptor for herbivore-associated molecular patterns mediates plant immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-06-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/693291v1?rss=1">
<title>
<![CDATA[
An N-terminal motif in NLR immune receptors is functionally conserved across distantly related plant species 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/693291v1?rss=1"
</link>
<description><![CDATA[
The molecular codes underpinning the functions of plant NLR immune receptors are poorly understood. We used in vitro Mu transposition to generate a random truncation library and identify the minimal functional region of NLRs. We applied this method to NRC4--a helper NLR that functions with multiple sensor NLRs within a Solanaceae receptor network. This revealed that the NRC4 N-terminal 29 amino acids are sufficient to induce hypersensitive cell death. This region is defined by the consensus MADAxVSFxVxKLxxLLxxEx (MADA motif) that is conserved at the N-termini of NRC family proteins and ~20% of coiled-coil (CC)-type plant NLRs. The MADA motif matches the N-terminal 1 helix of Arabidopsis NLR protein ZAR1, which undergoes a conformational switch during resistosome activation. Immunoassays revealed that the MADA motif is functionally conserved across NLRs from distantly related plant species. NRC-dependent sensor NLRs lack MADA sequences indicating that this motif has degenerated in sensor NLRs over evolutionary time.
]]></description>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Contreras, M.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Duggan, C.</dc:creator>
<dc:creator>Moratto, E.</dc:creator>
<dc:creator>Bozkurt, T.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2019-07-04</dc:date>
<dc:identifier>doi:10.1101/693291</dc:identifier>
<dc:title><![CDATA[An N-terminal motif in NLR immune receptors is functionally conserved across distantly related plant species]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-07-04</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/701359v1?rss=1">
<title>
<![CDATA[
Estradiol-inducible AvrRps4 expression reveals distinct properties of TIR-NLR-mediated effector-triggered immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/701359v1?rss=1"
</link>
<description><![CDATA[
Plant nucleotide-binding domain, leucine-rich repeat receptor (NLR) proteins play important roles in recognition of pathogen-derived effectors. However, the mechanism by which plant NLRs activate immunity is still largely unknown. The paired Arabidopsis NLRs RRS1-R and RPS4, that confer recognition of bacterial effectors AvrRps4 and PopP2, are well studied, but how the RRS1/RPS4 complex activates early immediate downstream responses upon effector detection is still poorly understood. To study RRS1/RPS4 responses without the influence of cell-surface receptor immune pathways, we generated an Arabidopsis line with inducible expression of effector AvrRps4. Induction does not lead to hypersensitive cell death response (HR) but can induce electrolyte leakage, which often correlates with plant cell death. Activation of RRS1 and RPS4 without pathogens cannot activate mitogen-associated protein kinase cascades, but still activates upregulation of defense genes, and therefore resistance against bacteria.nnHighlightInducible expression of AvrRps4 activates RRS1/RPS4-mediated effector-triggered immunity without the presence of pathogens, allowing us to characterise downstream immune responses triggered by TIR-NLRs without cell-surface receptor-mediated immunity.
]]></description>
<dc:creator>Ngou, B. P. M.</dc:creator>
<dc:creator>Ahn, H.-K.</dc:creator>
<dc:creator>Ding, P.</dc:creator>
<dc:creator>Redkar, A.</dc:creator>
<dc:creator>Brown, H.</dc:creator>
<dc:creator>Ma, Y.</dc:creator>
<dc:creator>Youles, M.</dc:creator>
<dc:creator>Tomlinson, L.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2019-07-14</dc:date>
<dc:identifier>doi:10.1101/701359</dc:identifier>
<dc:title><![CDATA[Estradiol-inducible AvrRps4 expression reveals distinct properties of TIR-NLR-mediated effector-triggered immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-07-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/697425v1?rss=1">
<title>
<![CDATA[
A CRISPR/Cas9 mediated 53 kb deletion of the NRC4 gene cluster of tomato does not affect bacterial flagellin-triggered immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/697425v1?rss=1"
</link>
<description><![CDATA[
Plants utilise cell surface pattern recognition receptors (PRRs) and intracellular nucleotide-binding domain leucine-rich repeat containing receptors (NLRs) to fend off invading pathogens. Although PRR- and NLR-triggered immunity are generally thought to activate distinct pathways, they can induce similar outputs. However, whether these two pathways converge at some point to potentiate and strengthen the immune response remains unclear. For instance, the extent to which the tomato NLR helper NRC4 is implicated in response to the bacterial flagellin peptide flg22 needs to be elucidated. One challenge is that the tomato NRC4 gene cluster consists of three paralogues and the related NRC5 gene. Here, we took advantage of the CRISPR/Cas9 system to generate a tomato mutant with a 53 kb deletion that encompasses the four NRC genes. Although this mutant failed to respond to the NRC4-dependent NLR Rpi-blb2, it remained unaltered in flg22-induced responses. We conclude that the NRC4 genes are not essential for flg22-induced responses in tomato.
]]></description>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Castells-Graells, R.</dc:creator>
<dc:creator>Nekrasov, V.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2019-07-10</dc:date>
<dc:identifier>doi:10.1101/697425</dc:identifier>
<dc:title><![CDATA[A CRISPR/Cas9 mediated 53 kb deletion of the NRC4 gene cluster of tomato does not affect bacterial flagellin-triggered immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-07-10</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/775973v1?rss=1">
<title>
<![CDATA[
High-resolution Expression Profiling of Selected Gene Sets during Plant Immune Activation 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/775973v1?rss=1"
</link>
<description><![CDATA[
Sequence capture followed by next-generation sequencing has broad applications in cost-effective exploration of biological processes at high resolution [1, 2]. Genome-wide RNA sequencing (RNA-seq) over a time course can reveal the dynamics of differential gene expression. However, in many cases, only a limited set of genes are of interest, and are repeatedly used as markers for certain biological processes. Sequence capture can help generate high-resolution quantitative datasets to assess changes in abundance of selected genes. We previously used sequence capture to accelerate Resistance gene cloning [1, 3, 4], investigate immune receptor gene diversity [5] and investigate pathogen diversity and evolution [6, 7].nnThe plant immune system involves detection of pathogens via both cell-surface and intracellular receptors. Both receptor classes can induce transcriptional reprogramming that elevates disease resistance [8]. To assess differential gene expression during plant immunity, we developed and deployed quantitative sequence capture (CAP-I). We designed and synthesized biotinylated single-strand RNA bait libraries targeted to a subset of defense genes, and generated sequence capture data from 99 RNA-seq libraries. We built a data processing pipeline to quantify the RNA-CAP-I-seq data, and visualize differential gene expression. Sequence capture in combination with quantitative RNA-seq enabled cost-effective assessment of the expression profile of a specified subset of genes. Quantitative sequence capture is not limited to RNA-seq or any specific organism and can potentially be incorporated into automated platforms for high-throughput sequencing.
]]></description>
<dc:creator>Ding, P.</dc:creator>
<dc:creator>Ngou, B. P. M.</dc:creator>
<dc:creator>Furzer, O. J.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Shrestha, R. K.</dc:creator>
<dc:creator>MacLean, D.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2019-09-23</dc:date>
<dc:identifier>doi:10.1101/775973</dc:identifier>
<dc:title><![CDATA[High-resolution Expression Profiling of Selected Gene Sets during Plant Immune Activation]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-09-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/780890v1?rss=1">
<title>
<![CDATA[
Intra-strain elicitation and suppression of plant immunity by Ralstonia solanacearum type-III effectors in Nicotiana benthamiana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/780890v1?rss=1"
</link>
<description><![CDATA[
Effector proteins delivered inside plant cells are powerful weapons for bacterial pathogens, but this exposes the pathogen to potential recognition by the plant immune system. Therefore, the effector repertoire of a given pathogen must be balanced for a successful infection. Ralstonia solanacearum is an aggressive pathogen with a large repertoire of secreted effectors. One of these effectors, RipE1, is conserved in most R. solanacearum strains sequenced to date. In this work, we found that RipE1 triggers immunity in N. benthamiana, which requires the immune regulator SGT1, but not EDS1 or NRCs. Interestingly, RipE1-triggered immunity induces the accumulation of salicylic acid (SA) and the overexpression of several genes encoding phenylalanine-ammonia lyases (PALs), suggesting that the unconventional PAL-mediated pathway is responsible for the observed SA biosynthesis. Surprisingly, RipE1 recognition also induces the expression of jasmonic acid (JA)-responsive genes and JA biosynthesis, suggesting that both SA and JA may act cooperatively in response to RipE1. Finally, we found that RipE1 expression leads to the accumulation of glutathione in plant cells, which precedes the activation of immune responses. R. solanacearum encodes another effector, RipAY, which is known to inhibit immune responses by degrading cellular glutathione. Accordingly, we show that RipAY inhibits RipE1-triggered immune responses. This work shows a strategy employed by R. solanacearum to counteract the perception of its effector proteins by the plant immune system.
]]></description>
<dc:creator>Sang, Y.</dc:creator>
<dc:creator>Yu, W.</dc:creator>
<dc:creator>Zhuang, H.</dc:creator>
<dc:creator>Wei, Y.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Luo, J.</dc:creator>
<dc:creator>Macho, A.</dc:creator>
<dc:date>2019-09-24</dc:date>
<dc:identifier>doi:10.1101/780890</dc:identifier>
<dc:title><![CDATA[Intra-strain elicitation and suppression of plant immunity by Ralstonia solanacearum type-III effectors in Nicotiana benthamiana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-09-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/839308v1?rss=1">
<title>
<![CDATA[
An rpw8 quadruple mutant of Arabidopsis Col-0 is partially compromised in bacterial and fungal resistance 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/839308v1?rss=1"
</link>
<description><![CDATA[
The plant immune system relies on both cell-surface and intracellular NLR (nucleotide-binding, leucine-rich repeat) receptors. NLRs respond to pathogen effectors and activate effector-triggered immunity: a cocktail of responses, often accompanied by cell death, resulting in resistance.

RPW8 encodes an unusual non-NLR Resistance (R) protein and confers broad-spectrum powdery mildew resistance. It requires genetic components also required by some NLRs, resembles the HeLo-containing protein MLKL (necroptosis executor in animals) and HET-S (cell death executor in fungi) and is targeted to the extra-haustorial membrane during powdery mildew infection by its N-terminal non-cleaved signal anchor domain. RPW8 displays extensive recent duplication events in Arabidopsis and certain alleles can induce oligomerisation-dependent activation of the NLR RPP7.

All these features enabled us to formulate hypotheses for RPW8 function: (1) RPW8 could be a cell death executor for defence against pathogens. (2) RPW8 could be a decoy for effector targets.

To test these hypotheses, we generated a quadruple knock-out mutant of the four RPW8-homologous copies in Arabidopsis Col-0, using CRISPR. The mutant still displays cell death upon activation of four well-characterised NLRs. However, it is partially impaired in powdery mildew resistance and also in bacterial resistance. Interestingly Col-0_rpw8 is delayed in flowering transition. In conclusion, RPW8 plays a broad role in immunity and plant development, beyond resistance to powdery mildew. There is no evidence that it is involved in executing ETI-associated cell death.
]]></description>
<dc:creator>Castel, B.</dc:creator>
<dc:creator>Wu, Y.</dc:creator>
<dc:creator>Xiao, S.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2019-11-12</dc:date>
<dc:identifier>doi:10.1101/839308</dc:identifier>
<dc:title><![CDATA[An rpw8 quadruple mutant of Arabidopsis Col-0 is partially compromised in bacterial and fungal resistance]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-11-12</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2019.12.16.878272v1?rss=1">
<title>
<![CDATA[
Cleavage of a pathogen apoplastic protein by plant subtilases activates immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2019.12.16.878272v1?rss=1"
</link>
<description><![CDATA[
The plant apoplast is a harsh environment in which hydrolytic enzymes, especially proteases, accumulate during pathogen infection. However, the defense functions of most apoplastic proteases remains largely elusive. Here, we show that a newly identified small cysteine-rich secreted protein PC2 from the potato late blight pathogen Phytophthora infestans induces immunity in Solanum plant species only after cleavage by plant apoplastic subtilisin-like proteases, such as tomato P69B. A minimal 61-amino-acid core peptide carrying two key cysteines and widely conserved among most oomycete species is sufficient for PC2 activity. Kazal-like protease inhibitors, such as EPI1 produced by P. infestans can prevent PC2 cleavage and dampen PC2 elicited host immunity. This study reveals that cleavage of pathogen proteins to release immunogenic peptides is an important function of apoplastic proteases but that pathogens interfere with these functions using protease inhibitor effectors.
]]></description>
<dc:creator>Wang, S.</dc:creator>
<dc:creator>Xing, R.</dc:creator>
<dc:creator>Wang, Y.</dc:creator>
<dc:creator>Shu, H.</dc:creator>
<dc:creator>Fu, S.</dc:creator>
<dc:creator>Paulus, J.</dc:creator>
<dc:creator>Schuster, M.</dc:creator>
<dc:creator>Saunders, D.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Vleeshouwers, V.</dc:creator>
<dc:creator>Zheng, X.</dc:creator>
<dc:creator>van der Hoorn, R. A. L.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Dong, S.</dc:creator>
<dc:date>2019-12-17</dc:date>
<dc:identifier>doi:10.1101/2019.12.16.878272</dc:identifier>
<dc:title><![CDATA[Cleavage of a pathogen apoplastic protein by plant subtilases activates immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2019-12-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.01.10.901983v1?rss=1">
<title>
<![CDATA[
Genomic rearrangements generate hypervariable mini-chromosomes in host-specific lineages of the blast fungus 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.01.10.901983v1?rss=1"
</link>
<description><![CDATA[
Supernumerary mini-chromosomes-a unique type of genomic structural variation-have been implicated in the emergence of virulence traits in plant pathogenic fungi. However, the mechanisms that facilitate the emergence and maintenance of mini-chromosomes across fungi remain poorly understood. In the blast fungus Magnaporthe oryzae, mini-chromosomes have been first described in the early 1990s but, until very recently, have been overlooked in genomic studies. Here we investigated structural variation in four isolates of the blast fungus M. oryzae from different grass hosts and analyzed the sequences of mini-chromosomes in the rice, foxtail millet and goosegrass isolates. The mini-chromosomes of these isolates turned out to be highly diverse with distinct sequence composition. They are enriched in repetitive elements and have lower gene density than core-chromosomes. We identified several virulence-related genes in the mini-chromosome of the rice isolate, including the polyketide synthase Ace1 and the effector gene AVR-Pik. Macrosynteny analyses around these loci revealed structural rearrangements, including inter-chromosomal translocations between core- and mini-chromosomes. Our findings provide evidence that mini-chromosomes independently emerge from structural rearrangements of core-chromosomes and might contribute to adaptive evolution of the blast fungus.

Author summaryThe genomes of plant pathogens often exhibit an architecture that facilitates high rates of dynamic rearrangements and genetic diversification in virulence associated regions. These regions, which tend to be gene sparse and repeat rich, are thought to serve as a cradle for adaptive evolution. Supernumerary chromosomes, i.e. chromosomes that are only present in some but not all individuals of a species, are a special type of structural variation that have been observed in plants, animals, and fungi. Here we identified and studied supernumerary mini-chromosomes in the blast fungus Magnaporthe oryzae, a pathogen that causes some of the most destructive plant diseases. We found that rice, foxtail millet and goosegrass isolates of this pathogen contain mini-chromosomes with distinct sequence composition. All mini-chromosomes are rich in repetitive genetic elements and have lower gene densities than core-chromosomes. Further, we identified virulence-related genes on the mini-chromosome of the rice isolate. We observed large-scale genomic rearrangements around these loci, indicative of a role of mini-chromosomes in facilitating genome dynamics. Taken together, our results indicate that mini-chromosomes facilitate genome rearrangements and possibly adaptive evolution of the blast fungus.
]]></description>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Gomez-Luciano, L. B.</dc:creator>
<dc:creator>Shrestha, R. K.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2020-01-11</dc:date>
<dc:identifier>doi:10.1101/2020.01.10.901983</dc:identifier>
<dc:title><![CDATA[Genomic rearrangements generate hypervariable mini-chromosomes in host-specific lineages of the blast fungus]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-01-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.01.09.900308v1?rss=1">
<title>
<![CDATA[
Recently expanded clonal lineages of the rice blast fungus display distinct patterns of presence/absence of effector genes 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.01.09.900308v1?rss=1"
</link>
<description><![CDATA[
BackgroundUnderstanding the mechanisms and timescales of plant pathogen outbreaks requires a detailed genome-scale analysis of their population history. The fungus Magnaporthe (Syn. Pyricularia) oryzae --the causal agent of blast disease of cereals-- is among the most destructive plant pathogens to world agriculture and a major threat to the production of rice, wheat and other cereals. Although M. oryzae is a multihost pathogen that infects more than 50 species of cereals and grasses, all rice-infecting isolates belong to a single genetically defined lineage. Here, we combined multiple genomics datasets to reconstruct the genetic history of the rice-infecting lineage of M. oryzae based on 131 isolates from 21 countries.

ResultsThe global population of the rice blast fungus consists of a diverse set of individuals and three well-defined genetic groups. Multiple population genetic tests revealed that the rice-infecting lineage of the blast fungus probably originated from a recombining diverse group in South East Asia followed by three independent clonal expansions that took place over the last [~]200 years. Patterns of allele sharing identified a subpopulation from the recombining diverse group that introgressed with one of the clonal lineages before its global expansion. Remarkably, the four genetic lineages of the rice blast fungus vary in the number and patterns of presence/absence of candidate effector genes. In particular, clonal lineages carry a reduced repertoire of effector genes compared with the diverse group, and specific combinations of effector presence/absence define each of the pandemic clonal lineages.

ConclusionsOur analyses reconstruct the genetic history of the rice-infecting lineage of M. oryzae revealing three clonal lineages associated with rice blast pandemics. Each of these lineages displays a specific pattern of presence/absence of effector genes that may have shaped their adaptation to the rice host and their evolutionary history.
]]></description>
<dc:creator>Latorre, S. M.</dc:creator>
<dc:creator>Reyes-Avila, C. S.</dc:creator>
<dc:creator>Malmgren, A.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Burbano, H. A.</dc:creator>
<dc:date>2020-01-10</dc:date>
<dc:identifier>doi:10.1101/2020.01.09.900308</dc:identifier>
<dc:title><![CDATA[Recently expanded clonal lineages of the rice blast fungus display distinct patterns of presence/absence of effector genes]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-01-10</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.02.05.936203v1?rss=1">
<title>
<![CDATA[
A hierarchical transcriptional network controls appressorium-mediated plant infection by the rice blast fungus Magnaporthe oryzae 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.02.05.936203v1?rss=1"
</link>
<description><![CDATA[
Rice blast is a pervasive and devastating disease that threatens rice production across the world. In spite of its importance to global food security, however, the underlying biology of plant infection by the blast fungus Magnaporthe oryzae remains poorly understood. In particular, it is unclear how the fungus elaborates a specialised infection cell, the appressorium, in response to surface signals from the rice leaf. Here, we report the identification of a network of temporally co-regulated transcription factors that act downstream of the Pmk1 mitogen-activated protein kinase pathway to regulate gene expression during appressorium-mediated plant infection. We have functionally characterised this network of transcription factors and demonstrated the operation of a hierarchical transcriptional control system. We show that this tiered regulatory mechanism involves Pmk1-dependent phosphorylation of the Hox7 homeobox transcription factor, which represses hyphal-associated gene expression and simultaneously induces major physiological changes required for appressorium development, including cell cycle arrest, autophagic cell death, turgor generation and melanin biosynthesis. Mst12 then regulates gene functions involved in septin-dependent cytoskeletal re-organisation, polarised exocytosis and effector gene expression necessary for plant tissue invasion.
]]></description>
<dc:creator>Oses-Ruiz, M.</dc:creator>
<dc:creator>Martin-Urdiroz, M.</dc:creator>
<dc:creator>Soanes, D. M.</dc:creator>
<dc:creator>Kershaw, M. J.</dc:creator>
<dc:creator>Cruz-Mireles, N.</dc:creator>
<dc:creator>Valdovinos-Ponce, G.</dc:creator>
<dc:creator>Molinari, C.</dc:creator>
<dc:creator>Littlejohn, G. R.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Valent, B.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:date>2020-02-06</dc:date>
<dc:identifier>doi:10.1101/2020.02.05.936203</dc:identifier>
<dc:title><![CDATA[A hierarchical transcriptional network controls appressorium-mediated plant infection by the rice blast fungus Magnaporthe oryzae]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-02-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.03.20.000117v1?rss=1">
<title>
<![CDATA[
The Irish potato famine pathogen subverts host vesicle trafficking to channel starvation-induced autophagy to the pathogen interface 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.03.20.000117v1?rss=1"
</link>
<description><![CDATA[
Eukaryotic cells deploy autophagy to eliminate invading microbes. In turn, pathogens have evolved effector proteins to counteract antimicrobial autophagy. How and why adapted pathogens co-opt autophagy for their own benefit is poorly understood. The Irish famine pathogen Phythophthora infestans secretes the effector protein PexRD54 that selectively activates an unknown plant autophagy pathway, while antagonizing antimicrobial autophagy. Here we show that PexRD54 induces autophagosome formation by bridging small GTPase Rab8a-decorated vesicles with autophagic compartments labelled by the core autophagy protein ATG8CL. Rab8a is required for pathogen-triggered and starvation-induced but not antimicrobial autophagy, revealing that specific trafficking pathways underpin selective autophagy. We discovered that Rab8a contributes to basal immunity against P. infestans, but PexRD54 diverts a sub-population of Rab8a vesicles to lipid droplets that associate with autophagosomes. These are then diverted towards pathogen feeding structures that are accommodated within the host cells. We propose that PexRD54 mimics starvation-induced autophagy by channeling host endomembrane trafficking towards the pathogen interface possibly to acquire nutrients. This work reveals that effectors can interconnect independent host compartments to stimulate complex cellular processes that benefit the pathogen.

Graphical abstract

O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=200 SRC="FIGDIR/small/000117v1_ufig1.gif" ALT="Figure 1">
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]]></description>
<dc:creator>Pandey, P.</dc:creator>
<dc:creator>Leary, A. Y.</dc:creator>
<dc:creator>Tümtas, Y.</dc:creator>
<dc:creator>Savage, Z.</dc:creator>
<dc:creator>Dagvadorj, B.</dc:creator>
<dc:creator>Tan, E.</dc:creator>
<dc:creator>Khandare, V.</dc:creator>
<dc:creator>Duggan, C.</dc:creator>
<dc:creator>Yusunov, T.</dc:creator>
<dc:creator>Madalinski, M.</dc:creator>
<dc:creator>Gabriel Mirkin, F.</dc:creator>
<dc:creator>Schornack, S.</dc:creator>
<dc:creator>Dagdas, Y.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:date>2020-03-21</dc:date>
<dc:identifier>doi:10.1101/2020.03.20.000117</dc:identifier>
<dc:title><![CDATA[The Irish potato famine pathogen subverts host vesicle trafficking to channel starvation-induced autophagy to the pathogen interface]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-03-21</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.04.10.034173v1?rss=1">
<title>
<![CDATA[
Mutual Potentiation of Plant Immunity by Cell-surface and Intracellular Receptors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.04.10.034173v1?rss=1"
</link>
<description><![CDATA[
The plant immune system involves cell-surface receptors that detect intercellular pathogen-derived molecules, and intracellular receptors that activate immunity upon detection of pathogen-secreted effectors that act inside the plant cell. Surface receptor-mediated immunity has been extensively studied but in authentic interactions between plants and microbial pathogens, its presence impedes study of intracellular receptor-mediated immunity alone. How these two immune pathways interact is poorly understood. Here, we reveal mutual potentiation between these two recognition-dependent defense pathways. Recognition by surface receptors activates multiple protein kinases and NADPH oxidases, whereas intracellular receptors primarily elevate abundance of these proteins. Reciprocally, the intracellular receptor-dependent hypersensitive cell death response is strongly enhanced by activation of surface receptors. Activation of either immune system alone is insufficient to provide effective resistance against Pseudomonas syringae. Thus, immune pathways activated by cell-surface and intracellular receptors mutually potentiate to activate strong defense that thwarts pathogens. By studying the activation of intracellular receptors in the absence of surface receptor-mediated immunity, we have dissected the relationship between the two distinct immune systems. These findings reshape our understanding of plant immunity and have broad implications for crop improvement.
]]></description>
<dc:creator>Ngou, B. P. M.</dc:creator>
<dc:creator>Ahn, H.-K.</dc:creator>
<dc:creator>Ding, P.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2020-04-10</dc:date>
<dc:identifier>doi:10.1101/2020.04.10.034173</dc:identifier>
<dc:title><![CDATA[Mutual Potentiation of Plant Immunity by Cell-surface and Intracellular Receptors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-04-10</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.04.27.062893v1?rss=1">
<title>
<![CDATA[
Conserved Molecular Function and Regulatory Subfunctionalization of the LORELEI Gene Family in Brassicaceae 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.04.27.062893v1?rss=1"
</link>
<description><![CDATA[
A signaling complex comprising members of the LORELEI (LRE)-LIKE GPI-anchored protein (LLG) and Catharanthus roseus RECEPTOR-LIKE KINASE 1-LIKE (CrRLK1L) families perceive RAPID ALKALINIZATION FACTOR (RALF) peptides and regulate growth, reproduction, immunity, and stress responses in Arabidopsis. Genes encoding these proteins are members of multi-gene families in most angiosperms and could generate thousands of signaling complex variants. However, the link(s) between expansion of these gene families and the functional diversification of this critical signaling complex as well as the evolutionary factors underlying the maintenance of gene duplicates remain unknown. Here, we investigated LLG gene family evolution, function, and expression in angiosperms. We found that LLGs in monocots and eudicots are descendants of a duplication early in angiosperm evolution and that both ancient and recent LLG duplicates are retained. Complementation and expression analysis showed that expression divergence of LLGs (regulatory subfunctionalization), rather than functional divergence, explains the retention of paralogs in Brassicales. All but one extant monocot and eudicot species examined maintained an LLG copy with preferential expression in male reproductive tissues, with the other duplicate copies showed highest levels of expression in female or vegetative tissues. Interestingly, the single LLG copy in Amborella (sister to all other angiosperms) is expressed vastly higher in male compared to female reproductive or vegetative tissues. Reconstruction of expression evolution showed that the highest inferred expression levels for the single copy ancestral angiosperm LLG was in male reproductive tissues. We propose that expression divergence played an important role in maintenance of LLG duplicates in angiosperms.

One Sentence SummaryExpression divergence played an important role in maintenance of two sub-groups of LLG duplicates in angiosperms
]]></description>
<dc:creator>Noble, J. A.</dc:creator>
<dc:creator>Liu, M.-C. J.</dc:creator>
<dc:creator>DeFalco, T. A.</dc:creator>
<dc:creator>Stegmann, M.</dc:creator>
<dc:creator>McNamara, K.</dc:creator>
<dc:creator>Sullivan, B.</dc:creator>
<dc:creator>Dinh, K. K.</dc:creator>
<dc:creator>Khuu, N.</dc:creator>
<dc:creator>Hancock, S.</dc:creator>
<dc:creator>Shiu, S.-H.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Beilstein, M. A.</dc:creator>
<dc:creator>Cheung, A. Y.</dc:creator>
<dc:creator>Palanivelu, R.</dc:creator>
<dc:date>2020-04-29</dc:date>
<dc:identifier>doi:10.1101/2020.04.27.062893</dc:identifier>
<dc:title><![CDATA[Conserved Molecular Function and Regulatory Subfunctionalization of the LORELEI Gene Family in Brassicaceae]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-04-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.05.11.086728v1?rss=1">
<title>
<![CDATA[
Lumi-Map, a real-time luciferase bioluminescence screen of mutants combined with MutMap, reveals Arabidopsis genes involved in PAMP-triggered immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.05.11.086728v1?rss=1"
</link>
<description><![CDATA[
Plants recognize pathogen-associated molecular patterns (PAMPs) to activate PAMP-triggered immunity (PTI). However, our knowledge of PTI signaling remains limited. In this report, we introduce Lumi-Map, a high-throughput platform for identifying causative single nucleotide polymorphisms (SNPs) to studying PTI signaling components. In Lumi-Map, a transgenic reporter plant line is produced that contains a firefly luciferase (LUC) gene driven by a defense gene promoter, which generates luminescence upon PAMP treatment. The line is mutagenized and the mutants with altered luminescence patterns are screened by a high-throughput real-time bioluminescence monitoring system. Selected mutants are subjected to MutMap analysis, a whole genome sequencing (WGS)-based method of rapid mutation identification, to identify the causative SNP responsible for the luminescence pattern change. We generated nine transgenic Arabidopsis reporter lines expressing LUC gene fused to multiple promoter sequences of defense-related genes. These lines generate luminescence upon activation of FLAGELLIN-SENSING 2 (FLS2) by flg22, a PAMP derived from bacterial flagellin. We selected the WRKY29-promoter reporter line to identify mutants in the signaling pathway downstream of FLS2. After screening 24,000 ethylmethanesulfonate (EMS)-induced mutants of the reporter line, we isolated 22 mutants with altered WRKY29 expression upon flg22 treatment (abbreviated as awf mutants). While five flg22-insensitive awf mutants harbored mutations in FLS2 itself, Lumi-Map revealed three genes not previously associated with PTI. Lumi-Map has the potential to identify novel PAMPs and their receptors as well as signaling components downstream of the receptors.
]]></description>
<dc:creator>Kato, H.</dc:creator>
<dc:creator>Onai, K.</dc:creator>
<dc:creator>Abe, A.</dc:creator>
<dc:creator>Shimizu, M.</dc:creator>
<dc:creator>Takagi, H.</dc:creator>
<dc:creator>Tateda, C.</dc:creator>
<dc:creator>Utsushi, H.</dc:creator>
<dc:creator>Singkarabanit-Ogawa, S.</dc:creator>
<dc:creator>Kitakura, S.</dc:creator>
<dc:creator>Ono, E.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Takano, Y.</dc:creator>
<dc:creator>Ishiura, M.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:date>2020-05-12</dc:date>
<dc:identifier>doi:10.1101/2020.05.11.086728</dc:identifier>
<dc:title><![CDATA[Lumi-Map, a real-time luciferase bioluminescence screen of mutants combined with MutMap, reveals Arabidopsis genes involved in PAMP-triggered immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-05-12</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.05.14.095158v1?rss=1">
<title>
<![CDATA[
Identification of Avramr1 from Phytophthora infestans using long read and cDNA pathogen-enrichment sequencing (PenSeq) 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.05.14.095158v1?rss=1"
</link>
<description><![CDATA[
O_LIPotato late blight, caused by the oomycete pathogen Phytophthora infestans, significantly hampers potato production. Recently, a new Resistance to Phytophthora infestans (Rpi) gene, Rpi-amr1, was cloned from a wild Solanum species, Solanum americanum. Identification of the corresponding recognized effector (Avirulence, or Avr) genes from P. infestans is key to elucidating their naturally occurring sequence variation, which in turn informs the potential durability of the cognate late blight resistance.
C_LIO_LITo identify the P. infestans effector recognized by Rpi-amr1, we screened available effector libraries and used long read and cDNA pathogen-enrichment sequencing (PenSeq) on four P. infestans isolates to explore the untested effectors.
C_LIO_LIBy using SMRT and cDNA PenSeq, we identified 47 highly expressed effectors from P. infestans, including PITG_07569 which triggers a highly specific cell death response when transiently co-expressed with Rpi-amr1 in Nicotiana benthamiana, suggesting that PITG_07569 is Avramr1.
C_LIO_LIHere we demonstrate that long read and cDNA PenSeq enables the identification of full-length RxLR effector families, and their expression profile. This study has revealed key insights into the evolution and polymorphism of a complex RxLR effector family that is associated with the recognition by Rpi-amr1.
C_LI
]]></description>
<dc:creator>Lin, X.</dc:creator>
<dc:creator>Song, T.</dc:creator>
<dc:creator>Fairhead, S.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Jouet, A.</dc:creator>
<dc:creator>Jupe, F.</dc:creator>
<dc:creator>Witek, A. I.</dc:creator>
<dc:creator>Vleeshouwers, V. G. A. A.</dc:creator>
<dc:creator>Hein, I.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:date>2020-05-14</dc:date>
<dc:identifier>doi:10.1101/2020.05.14.095158</dc:identifier>
<dc:title><![CDATA[Identification of Avramr1 from Phytophthora infestans using long read and cDNA pathogen-enrichment sequencing (PenSeq)]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-05-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.05.15.095497v1?rss=1">
<title>
<![CDATA[
A complex resistance locus in Solanum americanum recognizes a conserved Phytophthora effector 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.05.15.095497v1?rss=1"
</link>
<description><![CDATA[
Late blight caused by Phytophthora infestans greatly constrains potato production. Many Resistance (R) genes were cloned from wild Solanum species and/or introduced into potato cultivars by breeding. However, individual R genes have been overcome by P. infestans evolution; durable resistance remains elusive. We positionally cloned a new R gene, Rpi-amr1, from Solanum americanum, that encodes an NRC helper-dependent CC-NLR protein. Rpi-amr1 confers resistance in potato to all 19 P. infestans isolates tested. Using association genomics and long-read RenSeq, we defined eight additional Rpi-amr1 alleles from different S. americanum and related species. Despite only [~]90% identity between Rpi-amr1 proteins, all confer late blight resistance but differentially recognize Avramr1 orthologs and paralogs. We propose that Rpi-amr1 gene family diversity facilitates detection of diverse paralogs and alleles of the recognized effector, enabling broad-spectrum and durable resistance against P. infestans.
]]></description>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Lin, X.</dc:creator>
<dc:creator>Karki, H. S.</dc:creator>
<dc:creator>Jupe, F.</dc:creator>
<dc:creator>Witek, A. I.</dc:creator>
<dc:creator>Steuernagel, B.</dc:creator>
<dc:creator>Stam, R.</dc:creator>
<dc:creator>Van Oosterhout, C.</dc:creator>
<dc:creator>Fairhead, S.</dc:creator>
<dc:creator>Cocker, J. M.</dc:creator>
<dc:creator>Bhanvadia, S.</dc:creator>
<dc:creator>Barrett, W.</dc:creator>
<dc:creator>Song, T.</dc:creator>
<dc:creator>Vleeshouwers, V. G.</dc:creator>
<dc:creator>Tomlinson, L.</dc:creator>
<dc:creator>Wulff, B. B.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2020-05-16</dc:date>
<dc:identifier>doi:10.1101/2020.05.15.095497</dc:identifier>
<dc:title><![CDATA[A complex resistance locus in Solanum americanum recognizes a conserved Phytophthora effector]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-05-16</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.05.15.097584v1?rss=1">
<title>
<![CDATA[
A vector system for fast-forward in vivo studies of the ZAR1 resistosome in the model plant Nicotiana benthamiana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.05.15.097584v1?rss=1"
</link>
<description><![CDATA[
Nicotiana benthamiana has emerged as a complementary experimental system to Arabidopsis. It enables fast-forward in vivo analyses primarily through transient gene expression and is particularly popular in the study of plant immunity. Recently, our understanding of NLR plant immune receptors has greatly advanced following the discovery of Arabidopsis ZAR1 resistosome. Here, we describe a novel vector system of 52 plasmids that enables functional studies of the ZAR1 resistosome in N. benthamiana. We showed that ZAR1 stands out among the coiled coil class of NLRs for being highly conserved across distantly related dicot plant species and confirmed NbZAR1 as the N. benthamiana ortholog of Arabidopsis ZAR1. NbZAR1 triggers autoimmune cell death in N. benthamiana and this activity is dependent on a functional N-terminal 1 helix. C-terminally tagged NbZAR1 remains functional in N. benthamiana thus enabling cell biology and biochemical studies in this plant system. We conclude that the NbZAR1 open source plasmids form an additional experimental system to Arabidopsis for in planta resistosome studies.
]]></description>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:date>2020-05-16</dc:date>
<dc:identifier>doi:10.1101/2020.05.15.097584</dc:identifier>
<dc:title><![CDATA[A vector system for fast-forward in vivo studies of the ZAR1 resistosome in the model plant Nicotiana benthamiana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-05-16</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.05.15.098657v1?rss=1">
<title>
<![CDATA[
Chitosan inhibits septin-mediated plant infection by the rice blast fungus Magnaporthe oryzae in a Protein Kinase C and Nox1 NADPH oxidase-dependent manner 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.05.15.098657v1?rss=1"
</link>
<description><![CDATA[
O_LIChitosan is a partially deacetylated linear polysaccharide composed of {beta}-1,4-linked units of D-glucosamine and N-acetyl glucosamine. As well as acting as a structural component of fungal cell walls, chitosan can be applied as a potent antifungal agent. However, the mode-of-action of chitosan in fungal pathogens is poorly understood.
C_LIO_LIHere, we report that chitosan is effective for control of rice blast disease. Chitosan application impairs growth of the blast fungus Magnaporthe oryzae and has a pronounced effect on appressorium-mediated plant infection. Chitosan inhibits septin-mediated F-actin re-modelling at the appressorium pore, thereby preventing re-polarisation of the infection cell and rice leaf cuticle penetration.
C_LIO_LIWe found that chitosan causes plasma membrane permeabilization of M. oryzae and affects NADPH oxidase-dependent synthesis of reactive oxygen species, essential for septin ring formation and fungal pathogenicity. Our data further show that the toxicity of chitosan to M. oryzae requires the protein kinase C-dependent cell wall integrity pathway and the Nox1 NADPH oxidase. A conditionally lethal, analogue (PP1)-sensitive mutant of Pkc1 is partially remediated for growth in the presence of chitosan and PP1, while {Delta}nox1 mutants increase their glucan/chitin cell wall ratio, rendering them resistant to chitosan.
C_LIO_LITaken together, our data show that chitosan is a potent fungicide for control of the rice blast fungus which involves the cell wall integrity pathway, disrupts plasma membrane and inhibits septin-mediated plant infection.
C_LI
]]></description>
<dc:creator>Lopez-Moya, F.</dc:creator>
<dc:creator>Martin-Urdiroz, M.</dc:creator>
<dc:creator>Oses-Ruiz, M.</dc:creator>
<dc:creator>Fricker, M. D.</dc:creator>
<dc:creator>Littlejohn, G. R.</dc:creator>
<dc:creator>Lopez-Llorca, L. V.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:date>2020-05-16</dc:date>
<dc:identifier>doi:10.1101/2020.05.15.098657</dc:identifier>
<dc:title><![CDATA[Chitosan inhibits septin-mediated plant infection by the rice blast fungus Magnaporthe oryzae in a Protein Kinase C and Nox1 NADPH oxidase-dependent manner]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-05-16</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.05.26.116731v1?rss=1">
<title>
<![CDATA[
Cloning of the rice Xo1 resistance gene and interaction of the Xo1 protein with the defense-suppressing Xanthomonas effector Tal2h 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.05.26.116731v1?rss=1"
</link>
<description><![CDATA[
The Xo1 locus in the heirloom rice variety Carolina Gold Select confers resistance to bacterial leaf streak and bacterial blight, caused by Xanthomonas oryzae pvs. oryzicola and oryzae, respectively. Resistance is triggered by pathogen-delivered transcription activator-like effectors (TALEs) independent of their ability to activate transcription, and is suppressed by variants called truncTALEs common among Asian strains. By transformation of the susceptible variety Nipponbare, we show that one of 14 nucleotide-binding, leucine-rich repeat (NLR) protein genes at the locus, with a zfBED domain, is the Xo1 gene. Analyses of published transcriptomes revealed that the Xo1-mediated response is similar to those of NLR resistance genes Pia and Rxo1 and distinct from that associated with induction of the executor resistance gene Xa23, and that a truncTALE dampens or abolishes activation of defense-associated genes by Xo1. In Nicotiana benthamiana leaves, fluorescently-tagged Xo1 protein, like TALEs and truncTALEs, localized to the nucleus. And, endogenous Xo1 specifically co-immunoprecipitated from rice leaves with a pathogen-delivered, epitope-tagged truncTALE. These observations suggest that suppression of Xo1-function by truncTALEs occurs through direct or indirect physical interaction. They further suggest that effector co-immunoprecipitation may be effective for identifying or characterizing other resistance genes.
]]></description>
<dc:creator>Read, A. C.</dc:creator>
<dc:creator>Hutin, M. C.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:creator>Rinaldi, F. C.</dc:creator>
<dc:creator>Bogdanove, A. J.</dc:creator>
<dc:date>2020-05-29</dc:date>
<dc:identifier>doi:10.1101/2020.05.26.116731</dc:identifier>
<dc:title><![CDATA[Cloning of the rice Xo1 resistance gene and interaction of the Xo1 protein with the defense-suppressing Xanthomonas effector Tal2h]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-05-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.06.17.157040v1?rss=1">
<title>
<![CDATA[
Chromatin accessibility landscapes activated by cell surface and intracellular immune receptors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.06.17.157040v1?rss=1"
</link>
<description><![CDATA[
Activation of cell Surface and Intracellular Receptor-Mediated Immunity (SRMI and IRMI) results in rapid transcriptional reprogramming that underpins disease resistance. However, the mechanisms by which SRMI and IRMI lead to transcriptional changes are not clear. Here, we combine RNA-seq and ATAC-seq to define changes in gene expression and chromatin accessibility; both SRMI and IRMI increase chromatin accessibility at induced defense genes. Analysis of ATAC-seq and RNA-seq data combined with publicly available information on transcription factor DNA-binding motifs enabled comparison of individual gene regulatory networks activated by SRMI and IRMI, and by both. These results and analyses reveal overlapping and conserved transcriptional regulatory mechanism between the two immune systems.
]]></description>
<dc:creator>Ding, P.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Shrestha, R. K.</dc:creator>
<dc:creator>Perez, N. M.</dc:creator>
<dc:creator>Guo, W.</dc:creator>
<dc:creator>Ngou, B. P. M.</dc:creator>
<dc:creator>He, S.</dc:creator>
<dc:creator>Liu, C.</dc:creator>
<dc:creator>Feng, X.</dc:creator>
<dc:creator>Zhang, R.</dc:creator>
<dc:creator>Vandepoele, K.</dc:creator>
<dc:creator>MacLean, D.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2020-06-18</dc:date>
<dc:identifier>doi:10.1101/2020.06.17.157040</dc:identifier>
<dc:title><![CDATA[Chromatin accessibility landscapes activated by cell surface and intracellular immune receptors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-06-18</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.06.20.162834v1?rss=1">
<title>
<![CDATA[
The rice NLR pair Pikp-1/Pikp-2 initiates cell death through receptor cooperation rather than negative regulation 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.06.20.162834v1?rss=1"
</link>
<description><![CDATA[
Plant NLR immune receptors are multidomain proteins that can function as specialized sensor/helper pairs. Paired NLR immune receptors are generally thought to function via negative regulation, where one NLR represses the activity of the second and detection of pathogen effectors relieves this repression to initiate immunity. However, whether this mechanism is common to all NLR pairs is not known. Here, we show that the rice NLR pair Pikp-1/Pikp-2, which confers resistance to strains of the blast pathogen Magnaporthe oryzae (syn. Pyricularia oryzae) expressing the AVR-PikD effector, functions via receptor cooperation, with effector-triggered activation requiring both NLRs to trigger the immune response. To investigate the mechanism of Pikp-1/Pikp-2 activation, we expressed truncated variants of these proteins, and made mutations in previously identified NLR sequence motifs. We found that any domain truncation, in either Pikp-1 or Pikp-2, prevented cell death in the presence of AVR-PikD, revealing that all domains are required for activity. Further, expression of individual Pikp-1 or Pikp-2 domains did not result in cell death. Mutations in the conserved P-loop and MHD sequence motifs in both Pikp-1 and Pikp-2 prevented cell death activation, demonstrating that these motifs are required for the function of the two partner NLRs. Finally, we showed that Pikp-1 and Pikp-2 associate to form homo- and hetero-complexes in planta in the absence of AVR-PikD; on co-expression the effector binds to Pikp-1 generating a tripartite complex. Taken together, we provide evidence that Pikp-1 and Pikp-2 form a fine-tuned system that is activated by AVR-PikD via receptor cooperation rather than negative regulation.
]]></description>
<dc:creator>Zdrzalek, R.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2020-06-20</dc:date>
<dc:identifier>doi:10.1101/2020.06.20.162834</dc:identifier>
<dc:title><![CDATA[The rice NLR pair Pikp-1/Pikp-2 initiates cell death through receptor cooperation rather than negative regulation]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-06-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.06.22.164590v1?rss=1">
<title>
<![CDATA[
PacC-dependent adaptation and modulation of host cellular pH controls hemibiotrophic invasive growth and disease development by the rice blast fungus 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.06.22.164590v1?rss=1"
</link>
<description><![CDATA[
Many of the worlds most serious crop diseases are caused by hemibiotrophic fungi. These pathogens have evolved the ability to colonize living plant cells, suppressing plant immunity responses, before switching to necrotrophic growth, in which host cells die, providing the energy to fuel sporulation and spread of the fungus. How hemibiotrophic pathogens switch between these two lifestyles remains poorly understood. Here, we report that the devastating rice blast fungus, Magnaporthe oryzae, manipulates host cellular pH to regulate hemibiotrophy. During infection by M. oryzae, host plant cells are alkalinized to pH 7.8 during biotrophic growth, but later acidified to pH 6.5 during necrotrophy. Using a forward genetic screen, we identified alkaline-sensitive mutants of M. oryzae that were blocked in biotrophic proliferation and impaired in induction of host cell acidification and necrotrophy. These mutants defined components of the PacC-dependent ambient pH signal transduction pathway in M. oryzae. We report that PacC exists as a full-length repressor, PacC559, and a truncated transcriptional activator, PacC222, which localize to the fungal nucleus during biotrophic growth and to the cytoplasm during necrotrophy. During biotrophy, PacC222 directly activates genes associated with nutrient acquisition and fungal virulence, while PacC559 represses genes associated with saprophytic mycelial growth and sporulation, which are subsequently de-repressed during necrotrophy. When considered together, our results indicate that temporal regulation of hemibiotrophy by M. oryzae requires PacC-dependent sensing and manipulation of host cellular pH.

Author SummaryCrop diseases caused by fungi represent some of the most serious threats to global food security. Many fungal pathogens have evolved the ability to invade living plant tissue and suppress host immunity, before switching to a completely different mode of growth, in which they are able to kill host plant cells. This lifestyle- called hemibiotrophy -is exemplified by the blast fungus, Magnaporthe oryzae, which causes devastating diseases of rice, wheat and many other grasses. We found that during infection by M. oryzae, host cells initially have an alkaline pH, when the fungus is growing in living tissue, but pH rapidly becomes acidic, as host tissue is killed. We identified mutants of the blast fungus that were sensitive to alkaline pH and this enabled us to identify the signal transduction pathway by which the fungus responds to changes in ambient pH. We found that mutants in the pH response pathway were blocked in invasive fungal growth and could not cause acidification of host tissue. Consequently, they are unable to cause blast disease. We characterized the central regulator of this pathway, the PacC transcription factor, which unusually can act as both a repressor and an activator of fungal gene expression. During biotrophic invasive growth, PacC activates many genes previously reported to be required for virulence, including several associated with nutrient acquisition, and at the same time represses genes associated with vegetative growth and sporulation. The PacC signaling pathway is therefore necessary for regulating the switch in fungal lifestyle associated with causing blast disease.
]]></description>
<dc:creator>Chen, X.-L.</dc:creator>
<dc:creator>He, D.</dc:creator>
<dc:creator>Yin, C.</dc:creator>
<dc:creator>Yang, J.</dc:creator>
<dc:creator>Sun, J.</dc:creator>
<dc:creator>Wang, D.</dc:creator>
<dc:creator>Xue, M.</dc:creator>
<dc:creator>Li, Z.</dc:creator>
<dc:creator>Peng, Z.</dc:creator>
<dc:creator>Chen, D.</dc:creator>
<dc:creator>Zhao, W.</dc:creator>
<dc:creator>Xu, J.-R.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Peng, Y.-L.</dc:creator>
<dc:date>2020-06-22</dc:date>
<dc:identifier>doi:10.1101/2020.06.22.164590</dc:identifier>
<dc:title><![CDATA[PacC-dependent adaptation and modulation of host cellular pH controls hemibiotrophic invasive growth and disease development by the rice blast fungus]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-06-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.06.26.174169v1?rss=1">
<title>
<![CDATA[
Family-wide evaluation of RALF peptides in Arabidopsis thaliana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.06.26.174169v1?rss=1"
</link>
<description><![CDATA[
Plant peptide hormones are important players controlling various aspects of plants’ lives. RAPID ALKALINIZATION FACTOR (RALF) peptides have recently emerged as important players in multiple physiological processes. Numerous studies on RALF peptides focused on broad phylogenetic analysis including multiple species. Thus, progress has been made in understanding the evolutionary processes that shaped this family. Nevertheless, to date, there is no comprehensive, family-wide functional study on RALF peptides. Here, we analysed the phylogeny and function of the proposed multigenic RALF peptide family in the model plant Arabidopsis thaliana, ecotype Col-0. Our phylogenetic analysis reveals that two of the previously proposed RALF peptides are not genuine RALF peptides, which leads us to propose a new consensus AtRALF peptide family annotation. Moreover, we show that the majority of AtRALF peptides are able to induce seedling or root growth inhibition in A. thaliana seedlings when applied exogenously as synthetic peptides. Additionally, we show that most of these responses are dependent on the Catharanthus roseus RLK1-LIKE receptor kinase FERONIA, suggesting a pivotal role in the perception of multiple RALF peptides.One sentence summary The majority of A. thaliana RALF peptides inhibit growth in a FERONIA-dependent mannerView Full Text
]]></description>
<dc:creator>Abarca, A.</dc:creator>
<dc:creator>Franck, C. M.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2020-06-27</dc:date>
<dc:identifier>doi:10.1101/2020.06.26.174169</dc:identifier>
<dc:title><![CDATA[Family-wide evaluation of RALF peptides in Arabidopsis thaliana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-06-27</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.07.08.193250v1?rss=1">
<title>
<![CDATA[
Accurate plant pathogen effector protein classification ab initio with deepredeff, an ensemble of convolutional neural networks 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.07.08.193250v1?rss=1"
</link>
<description><![CDATA[
Plant pathogens cause billions of dollars of crop loss every year and are a major threat to global food security. Effector proteins are the tools such pathogens use to infect the cell, predicting effectors de novo from sequence is difficult because of the heterogeneity of the sequences. We hypothesised that deep learning classifiers based on Convolutional Neural Networks would be able to identify effectors and deliver new insights. We built a training set of manually curated effector sequences from PHI-Base and used these to train a range of model architectures for classifying bacteria, fungal and oomycete sequences. The best performing classifiers had accuracies from 93 % to 84 %. The models were tested against popular effector detection software on our own test data and data provided with those models. We observed better performance from our models. Specifically our models showed greater accuracy and lower tendencies to call false positives on a secreted protein negative test set and a greater generalisability. We used GRAD-CAM activation map analysis to identify the sequences that activated our CNN-LSTM models and found short but distinct N-terminal regions in each taxon that was indicative of effector sequences. No motifs could be observed in these regions but an analysis of amino acid types indicated differing patterns of enrichment and depletion that varied between taxa. We have produced an R package that will allow others to make easy effector predictions using our models.Competing Interest StatementThe authors have declared no competing interest.View Full Text
]]></description>
<dc:creator>Ruth Kristianingsih</dc:creator>
<dc:creator>Dan MacLean</dc:creator>
<dc:date>2020-07-09</dc:date>
<dc:identifier>doi:10.1101/2020.07.08.193250</dc:identifier>
<dc:title><![CDATA[Accurate plant pathogen effector protein classification ab initio with deepredeff, an ensemble of convolutional neural networks]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-07-09</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.07.08.193961v1?rss=1">
<title>
<![CDATA[
RefPlantNLR: a comprehensive collection of experimentally validated plant NLRs 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.07.08.193961v1?rss=1"
</link>
<description><![CDATA[
Reference datasets are critical in computational biology. They help define canonical biological features and are essential for benchmarking studies. Here, we describe a comprehensive reference dataset of experimentally validated plant NLR immune receptors. RefPlantNLR consists of 442 NLRs from 31 genera belonging to 11 orders of flowering plants. This reference dataset has several applications. We used RefPlantNLR to determine the canonical features of functionally validated plant NLRs and to benchmark the five most popular NLR annotation tools. This revealed that although NLR annotation tools tend to retrieve the majority of NLRs, they frequently produce domain architectures that are inconsistent with the RefPlantNLR annotation. Guided by this analysis, we developed a new pipeline, NLRtracker, which extracts and annotates NLRs based on the core features found in the RefPlantNLR dataset. The RefPlantNLR dataset should also prove useful for guiding comparative analyses of NLRs across the wide spectrum of plant diversity and identifying under-studied taxa. We hope that the RefPlantNLR resource will contribute to moving the field beyond a uniform view of NLR structure and function.
]]></description>
<dc:creator>Jiorgos Kourelis</dc:creator>
<dc:creator>Sophien Kamoun</dc:creator>
<dc:date>2020-07-09</dc:date>
<dc:identifier>doi:10.1101/2020.07.08.193961</dc:identifier>
<dc:title><![CDATA[RefPlantNLR: a comprehensive collection of experimentally validated plant NLRs]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-07-09</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.07.20.212233v1?rss=1">
<title>
<![CDATA[
FERONIA regulates FLS2 plasma membrane nanoscale dynamics to modulate plant immune signaling 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.07.20.212233v1?rss=1"
</link>
<description><![CDATA[
Spatial partitioning is a propensity of biological systems orchestrating cell activities in space and time. The dynamic regulation of plasma membrane nano-environments has recently emerged as a key fundamental aspect of plant signaling, but the molecular components governing it are still mostly unclear. The receptor kinase FERONIA (FER) controls complex formation of the immune receptor kinase FLAGELLIN SENSING 2 (FLS2) with its co-receptor BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1), and this function is inhibited by the FER ligand RAPID ALKALANIZATION FACTOR 23 (RALF23). Here, we show that FER regulates the plasma membrane nanoscale organization of FLS2 and BAK1. Our study demonstrates that akin to FER, leucine-rich repeat (LRR) extensin (LRXs) proteins contribute to RALF23 responsiveness, regulate BAK1 nanoscale organization and immune signaling. Furthermore, RALF23 perception leads to rapid modulation of FLS2 and BAK1 nanoscale organization and its inhibitory activity on immune signaling relies on FER kinase activity. Our results suggest that perception of RALF peptides by FER and LRXs actively modulates the plasma membrane nanoscale landscape to regulate cell surface signaling by other receptor kinases.
]]></description>
<dc:creator>zipfel, c.</dc:creator>
<dc:creator>Gronnier, J.</dc:creator>
<dc:creator>Franck, C. M.</dc:creator>
<dc:creator>Stegmann, M.</dc:creator>
<dc:creator>DeFalco, T.</dc:creator>
<dc:creator>Abarca, A.</dc:creator>
<dc:creator>Duenser, K.</dc:creator>
<dc:creator>Lin, W.</dc:creator>
<dc:creator>Yang, Z.</dc:creator>
<dc:creator>Kleine-Vehn, J.</dc:creator>
<dc:creator>Ringli, C.</dc:creator>
<dc:date>2020-07-21</dc:date>
<dc:identifier>doi:10.1101/2020.07.20.212233</dc:identifier>
<dc:title><![CDATA[FERONIA regulates FLS2 plasma membrane nanoscale dynamics to modulate plant immune signaling]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-07-21</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.09.16.299883v1?rss=1">
<title>
<![CDATA[
Large-scale identification of ubiquitination sites on membrane-associated proteins in Arabidopsis thaliana seedlings 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.09.16.299883v1?rss=1"
</link>
<description><![CDATA[
Protein phosphorylation and ubiquitination are two of the most abundant forms of post-translational modifications in eukaryotes, regulated by thousands of protein kinases, phosphatases, E3 ubiquitin ligases, and ubiquitin proteases. Although previous studies have catalogued several ubiquitinated proteins in plants (Walton et al., 2016), few membrane-localized proteins have been identified. Receptor kinases (RKs) initiate phosphorylation signal relays that regulate plant growth, development, and stress responses. While the regulatory role of phosphorylation on protein kinase function is well-documented (Couto and Zipfel, 2016), considerably less is known about the role of ubiquitination on protein kinase function, even though protein turnover is critical to their signaling competence and cellular homeostasis. Here we describe the large-scale identification of ubiquitination sites on Arabidopsis proteins associated with or integral to the plasma membrane, including over 100 protein kinases.
]]></description>
<dc:creator>Grubb, L.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Dunning, K.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Monaghan, J.</dc:creator>
<dc:date>2020-09-17</dc:date>
<dc:identifier>doi:10.1101/2020.09.16.299883</dc:identifier>
<dc:title><![CDATA[Large-scale identification of ubiquitination sites on membrane-associated proteins in Arabidopsis thaliana seedlings]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-09-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.09.24.308585v1?rss=1">
<title>
<![CDATA[
Host-interactor screens of Phytophthora infestans RXLR proteins reveal vesicle trafficking as a major effector-targeted process 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.09.24.308585v1?rss=1"
</link>
<description><![CDATA[
Pathogens modulate plant cell structure and function by secreting effectors into host tissues. Effectors typically function by associating with host molecules and modulating their activities. This study aimed to identify the host processes targeted by the RXLR class of host-translocated effectors of the potato blight pathogen Phytophthora infestans. To this end, we performed an in planta protein-protein interaction screen by transiently expressing P. infestans RXLR effectors in Nicotiana benthamiana leaves followed by co-immunoprecipitation (co-IP) and liquid chromatography tandem mass spectrometry (LC-MS/MS). This screen generated an effector-host protein interactome matrix of 59 P. infestans RXLR effectors x 586 N. benthamiana proteins. Classification of the host interactors into putative functional categories revealed over 35 biological processes possibly targeted by P. infestans. We further characterized the PexRD12/31 family of RXLR-WY effectors, which associate and co-localize with components of the vesicle trafficking machinery. One member of this family, PexRD31, increased the number of FYVE positive vesicles in N. benthamiana cells. FYVE positive vesicles also accumulated in leaf cells near P. infestans hyphae, indicating that the pathogen may enhance endosomal trafficking during infection. We anticipate that the interactome dataset we generated will serve as a useful community resource for functional studies of P. infestans effectors and of effector-targeted host processes.
]]></description>
<dc:creator>Petre, B.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Schattat, M. H.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Schornack, S.</dc:creator>
<dc:creator>Abd-El-Haliem, A.</dc:creator>
<dc:creator>Castells-Graells, R.</dc:creator>
<dc:creator>Lozano-Duran, R.</dc:creator>
<dc:creator>Dagdas, Y.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Jones, A. M. E.</dc:creator>
<dc:creator>Vossen, J.</dc:creator>
<dc:creator>Robatzek, S.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:date>2020-09-24</dc:date>
<dc:identifier>doi:10.1101/2020.09.24.308585</dc:identifier>
<dc:title><![CDATA[Host-interactor screens of Phytophthora infestans RXLR proteins reveal vesicle trafficking as a major effector-targeted process]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-09-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.10.08.331181v1?rss=1">
<title>
<![CDATA[
The Rpi-mcq1 resistance gene family recognizes Avr2 of Phytophthora infestans but is distinct from R2 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.10.08.331181v1?rss=1"
</link>
<description><![CDATA[
Potato late blight, which is caused by the destructive oomycete pathogen Phytophthora infestans, is a major threat to global food security. Several nucleotide binding, leucine-rich repeat (NLR) Resistance to P. infestans (Rpi) genes have been introgressed into potato cultivars from wild Solanum species that are native to Mexico, but these were quickly defeated. Positional cloning in Solanum mochiquense, combined with allele mining in Solanum huancabambense, were used to identify a new family of Rpi genes from Peruvian Solanum species. Rpi-mcq1, Rpi-hcb1.1 and Rpi-hcb1.2 confer race-specific resistance to a panel of P. infestans isolates. Effector assays showed that the Rpi-mcq1 family mediates a hypersensitive response upon recognition of the RXLR effector AVR2, which had previously been found to be exclusively recognized by the family of R2 resistance proteins. The Rpi-mcq1 and R2 genes are distinct and reside on chromosome IX and IV, respectively. This is the first report of two unrelated R protein families that recognize the same AVR protein. We anticipate that this likely is a consequence of a geographically separated dynamic co-evolution of R gene families of Solanum with an important effector gene of P. infestans.

Author summaryPotato is the largest non-grain staple crop and essential for food security world-wide. However, potato plants are continuously threatened by the notorious oomycete pathogen Phytophthora infestans that causes late blight. This devastating disease has led to the Irish famine more then 150 years ago, and is still a major threat for potato. Resistance against P. infestans can be found in wild relatives of potato, which carry resistance genes that belong to the nucleotide binding site-leucine-rich repeat (NLR) class. Known NLR proteins typically recognize a matching effector from Phytophthora, which leads to a hypersensitive resistance response (HR). For example, R2 from Mexican Solanum species recognizes AVR2 from P. infestans. So far, these R genes exclusively match to one Avr gene. Here, we identified a new class of NLR proteins that are different from R2, but also recognize the same effector AVR2. This new family of NLR occurs in South American Solanum species, and we anticipate that it is likely a product of a geographically separated co-evolution with AVR2. This is the first report of two unrelated R protein families that recognize the same AVR protein.
]]></description>
<dc:creator>Aguilera-Galvez, C.</dc:creator>
<dc:creator>Chu, Z.</dc:creator>
<dc:creator>Sumaiya Haque, O.</dc:creator>
<dc:creator>Wouters, D.</dc:creator>
<dc:creator>Gilroy, E.</dc:creator>
<dc:creator>Vossen, J.</dc:creator>
<dc:creator>Visser, R.</dc:creator>
<dc:creator>Birch, P.</dc:creator>
<dc:creator>Jones, J.</dc:creator>
<dc:creator>Vleeshouwers, V. G. A. A.</dc:creator>
<dc:date>2020-10-08</dc:date>
<dc:identifier>doi:10.1101/2020.10.08.331181</dc:identifier>
<dc:title><![CDATA[The Rpi-mcq1 resistance gene family recognizes Avr2 of Phytophthora infestans but is distinct from R2]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-10-08</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.10.12.333484v1?rss=1">
<title>
<![CDATA[
Jurassic NLR: conserved and dynamic evolutionary features of the atypically ancient immune receptor ZAR1 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.10.12.333484v1?rss=1"
</link>
<description><![CDATA[
In plants, NLR immune receptors generally exhibit hallmarks of rapid evolution even at the intraspecific level. We used iterative sequence similarity searches coupled with phylogenetic analyses to reconstruct the evolutionary history of ZAR1, an atypically conserved NLR that traces its origin to early flowering plant lineages [~]220 to 150 million years ago (Jurassic period). We discovered 120 ZAR1 orthologs in 88 species, including the monocot Colacasia esculenta, the magnoliid Cinnamomum micranthum and the majority of eudicots, notably the early diverging eudicot species Aquilegia coerulea. Ortholog sequence analyses revealed highly conserved features of ZAR1, including regions for pathogen effector recognition, intramolecular interactions and cell death activation. We functionally reconstructed the cell death activity of ZAR1 and its partner receptor-like cytoplasmic kinase (RLCK) from distantly related plant species, experimentally validating the hypothesis that ZAR1 has evolved to be a partner with RLCKs early in its evolution. In addition, ZAR1 acquired novel features, such as a C-terminal integration of a thioredoxin-like domain. ZAR1 duplicated into two paralog families, which underwent distinct evolutionary paths. We conclude that ZAR1 stands out among angiosperm NLRs for having experienced relatively limited gene duplication and expansion throughout its deep evolutionary history. Nonetheless, ZAR1 did also give rise to non-canonical NLR proteins with integrated domains and degenerated molecular features.
]]></description>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2020-10-12</dc:date>
<dc:identifier>doi:10.1101/2020.10.12.333484</dc:identifier>
<dc:title><![CDATA[Jurassic NLR: conserved and dynamic evolutionary features of the atypically ancient immune receptor ZAR1]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-10-12</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.10.25.354514v1?rss=1">
<title>
<![CDATA[
The Arabidopsis E3 ubiquitin ligase PUB4 regulates BIK1 homeostasis and is targeted by a bacterial type-III effector 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.10.25.354514v1?rss=1"
</link>
<description><![CDATA[
Plant immunity is tightly controlled by a complex and dynamic regulatory network, which ensures optimal activation upon detection of potential pathogens. Accordingly, each component of this network is a potential target for manipulation by pathogens. Here, we report that RipAC, a type III-secreted effector from the bacterial pathogen Ralstonia solanacearum, targets the plant E3 ubiquitin ligase PUB4 to inhibit pattern-triggered immunity (PTI). PUB4 plays a positive role in PTI by regulating the homeostasis of the central immune kinase BIK1. Before PAMP perception, PUB4 promotes the degradation of non-activated BIK1, while, after PAMP perception, PUB4 contributes to the accumulation of activated BIK1. RipAC leads to BIK1 degradation, which correlates with its PTI-inhibitory activity. RipAC causes a reduction in pathogen-associated molecular pattern (PAMP)-induced PUB4 accumulation and phosphorylation. Our results shed light on the role played by PUB4 in immune regulation, and illustrate an indirect targeting of the immune signalling hub BIK1 by a bacterial effector.
]]></description>
<dc:creator>Derkacheva, M.</dc:creator>
<dc:creator>Yu, G.</dc:creator>
<dc:creator>Rufian, J. S.</dc:creator>
<dc:creator>Jiang, S.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Morcillo, R.</dc:creator>
<dc:creator>Stransfeld, L.</dc:creator>
<dc:creator>Wei, Y.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Macho, A.</dc:creator>
<dc:date>2020-10-26</dc:date>
<dc:identifier>doi:10.1101/2020.10.25.354514</dc:identifier>
<dc:title><![CDATA[The Arabidopsis E3 ubiquitin ligase PUB4 regulates BIK1 homeostasis and is targeted by a bacterial type-III effector]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-10-26</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.11.06.371260v1?rss=1">
<title>
<![CDATA[
The host exocyst complex is targeted by a conserved bacterial type III effector protein that promotes virulence 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.11.06.371260v1?rss=1"
</link>
<description><![CDATA[
For most Gram-negative bacteria, pathogenicity largely depends on the type-III secretion system that delivers virulence effectors into eukaryotic cells. The subcellular targets for the majority of these effectors remain unknown. Here, we show that Xanthomonas campestris, the causal agent of black rot disease, delivers the highly conserved effector XopP that interacts with hosts EXO70 protein. EXO70 is an essential component of the exocyst complex with a role in plant immunity. The XopP/EXO70 interaction is specific and inhibits exocyst-dependent exocytosis without activating a specific plant NLR receptor that guards EXO70. In this way, Xanthomonas efficiently inhibits the hosts PAMP-triggered immunity (PTI) by blocking exocytosis of PR1, callose deposition and the FLS2 immunity-receptor translocation to the plasma membrane, promoting successful infection.
]]></description>
<dc:creator>A. Michalopoulou, V. A.</dc:creator>
<dc:creator>Kotsaridis, K.</dc:creator>
<dc:creator>Mermigka, G.</dc:creator>
<dc:creator>Kotsifaki, D.</dc:creator>
<dc:creator>Kokkinidis, M.</dc:creator>
<dc:creator>Celie, P. H. N.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:creator>Sarris, P. F.</dc:creator>
<dc:date>2020-11-07</dc:date>
<dc:identifier>doi:10.1101/2020.11.06.371260</dc:identifier>
<dc:title><![CDATA[The host exocyst complex is targeted by a conserved bacterial type III effector protein that promotes virulence]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-11-07</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.11.30.404566v1?rss=1">
<title>
<![CDATA[
The transcriptional landscape of Arabidopsis thaliana pattern-triggered immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.11.30.404566v1?rss=1"
</link>
<description><![CDATA[
Plants initiate immunity upon recognition of a wide array of self and non-self molecular patterns. Whether plants tune their immune outputs to patterns of different biological origins or of different biochemical nature remains mostly unclear. Here, we performed a detailed early time-series transcriptomics analysis in Arabidopsis thaliana, revealing that the response to diverse patterns is remarkably congruent. Early transcriptional reprogramming is dominated by a plant general stress response (GSR), which is essential for pattern-induced immunity. The definition of  core immunity response genes common and specific to pattern response in addition revealed the function of previously uncharacterized GLUTAMATE RECEPTOR-LIKE calcium-permeable channels in immunity. This study thus illustrates general and unique properties of early immune transcriptional reprogramming and uncovered important components of plant immunity.

One Sentence SummaryTime-resolved transcriptomics reveals new properties of pattern-triggered immunity and function of calcium-permeable channels.
]]></description>
<dc:creator>Bjornson, M.</dc:creator>
<dc:creator>Pimprikar, P.</dc:creator>
<dc:creator>Nuernberger, T.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2020-12-01</dc:date>
<dc:identifier>doi:10.1101/2020.11.30.404566</dc:identifier>
<dc:title><![CDATA[The transcriptional landscape of Arabidopsis thaliana pattern-triggered immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-12-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.12.01.403451v1?rss=1">
<title>
<![CDATA[
Multiple variants of the blast fungus effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19 with high affinity. 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.12.01.403451v1?rss=1"
</link>
<description><![CDATA[
Microbial plant pathogens secrete effector proteins which manipulate the host to promote infection. Effectors can be recognised by plant intracellular nucleotide-binding leucine-rich repeat (NLR) receptors, initiating an immune response. The AVR-Pik effector from the rice blast fungus Magnaporthe oryzae is recognised by a pair of rice NLR receptors, Pik-1 and Pik-2. Pik-1 contains a non-canonical integrated heavy metal-associated (HMA) domain, which directly binds AVR-Pik to activate plant defences. Non-canonical integrated domains are widespread in plant NLRs and are thought to resemble the host target of the recognised effector. AVR-Pik interacts with specific rice HMA domain-containing proteins, namely heavy metal-associated isoprenylated plant proteins (HIPPs) and heavy metal-associated plant proteins (HPPs). Here, we define the biochemical and structural basis of the interaction between AVR-Pik and OsHIPP19, and compare the interaction with the HMA domain of Pik-1. Using analytical gel filtration and surface plasmon resonance, we show that multiple AVR-Pik variants, including the stealthy variants AVR-PikC and AVR-PikF which do not interact with any characterised Pik-1 alleles, bind to OsHIPP19 with nanomolar affinity. The crystal structure of OsHIPP19 in complex with AVR-PikF reveals differences at the interface that underpin high-affinity binding of OsHIPP19-HMA to a wider set of AVR-Pik variants than achieved by the integrated HMA domain of Pik-1. Our results provide a foundation for engineering the HMA domain of Pik-1 to extend binding to currently unrecognised AVR-Pik variants and expand disease resistance in rice to divergent pathogen strains.
]]></description>
<dc:creator>Maidment, J. H. R.</dc:creator>
<dc:creator>Franceschetti, M.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>Jantasuriyarat, C.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2020-12-01</dc:date>
<dc:identifier>doi:10.1101/2020.12.01.403451</dc:identifier>
<dc:title><![CDATA[Multiple variants of the blast fungus effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19 with high affinity.]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-12-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.12.01.406389v1?rss=1">
<title>
<![CDATA[
The blast pathogen effector AVR-Pik binds and stabilizes rice heavy metal-associated (HMA) proteins to co-opt their function in immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.12.01.406389v1?rss=1"
</link>
<description><![CDATA[
Intracellular nucleotide-binding domain and leucine-rich repeat-containing (NLR) receptors play crucial roles in immunity across multiple domains of life. In plants, a subset of NLRs contain noncanonical integrated domains that are thought to have evolved from host targets of pathogen effectors to serve as pathogen baits. However, the functions of host proteins with similarity to NLR integrated domains and the extent to which they are targeted by pathogen effectors remain largely unknown. Here, we show that the blast fungus effector AVR-Pik binds a subset of related rice proteins containing a heavy metal-associated (HMA) domain, one of the domains that has repeatedly integrated into plant NLR immune receptors. We find that AVR-Pik binding stabilizes the rice small HMA (sHMA) proteins OsHIPP19 and OsHIPP20. Knockout of OsHIPP20 causes enhanced disease resistance towards the blast pathogen, indicating that OsHIPP20 is a susceptibility gene (S-gene). We propose that AVR-Pik has evolved to bind HMA domain proteins and co-opt their function to suppress immunity. Yet this binding carries a trade-off, it triggers immunity in plants carrying NLR receptors with integrated HMA domains.

Significance StatementRice blast disease, caused by the fungus Magnaporthe oryzae, is one of the most devastating diseases of rice. Therefore, understanding the mechanisms of blast fungus infection and resistance of rice against the disease is important for global food security. In this study, we show that the M. oryzae effector protein AVR-PikD binds rice sHMA proteins and stabilizes them, presumably to enhance pathogen infection. We show that loss-of-function mutants in one rice sHMA, OsHIPP20, reduced the level of susceptibility against a compatible isolate of M. oryzae, suggesting that M. oryzae requires host sHMA to facilitate invasion. Remarkably, OsHIPP20 knockout rice line showed no growth defect, suggesting editing sHMA genes may present a novel source of resistance against blast disease.
]]></description>
<dc:creator>Oikawa, K.</dc:creator>
<dc:creator>Fujisaki, K.</dc:creator>
<dc:creator>Shimizu, M.</dc:creator>
<dc:creator>Takeda, T.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>Hirabuchi, A.</dc:creator>
<dc:creator>Hiraka, Y.</dc:creator>
<dc:creator>Białas, A.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Kellner, R.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Cesari, S.</dc:creator>
<dc:creator>Kroj, T.</dc:creator>
<dc:creator>Maidment, J.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:date>2020-12-02</dc:date>
<dc:identifier>doi:10.1101/2020.12.01.406389</dc:identifier>
<dc:title><![CDATA[The blast pathogen effector AVR-Pik binds and stabilizes rice heavy metal-associated (HMA) proteins to co-opt their function in immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-12-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.12.18.423392v1?rss=1">
<title>
<![CDATA[
Rhamnolipids and their 3-(3-hydroxyalkanoyloxy)alkanoic acid precursors activate Arabidopsis innate immunity through two independent mechanisms 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.12.18.423392v1?rss=1"
</link>
<description><![CDATA[
Plant innate immunity is activated upon perception of invasion pattern molecules by plant cell-surface immune receptors. Several bacteria of the genera Pseudomonas and Burkholderia produce rhamnolipids (RLs) from L- rhamnose and (R)-3-hydroxyalkanoate precursors (HAAs). RL and HAA secretion is required to modulate bacterial surface motility, biofilm development, and thus successful colonization of hosts. Here, we show that the lipidic secretome from the opportunistic pathogen Pseudomonas aeruginosa mostly comprising RLs and HAAs stimulates Arabidopsis immunity. We demonstrate that HAAs are sensed by the bulb-type lectin receptor kinase LIPOOLIGOSACCHARIDE-SPECIFIC REDUCED ELICITATION/S-DOMAIN-1-29 (LORE/SD1-29) that also mediates medium-chain 3-hydroxy fatty acid (mc-3-OH-FA) perception in the plant Arabidopsis thaliana. HAA sensing induces canonical immune signaling and local resistance to plant pathogenic Pseudomonas infection. By contrast, RLs trigger an atypical immune response and resistance to Pseudomonas infection independent of LORE. Thus, the glycosyl moieties of RLs, albeit abolishing sensing by LORE, do not impair their ability to trigger plant defense. In addition, our results show that RL-triggered immune response is affected by the sphingolipid composition of the plasma membrane. In conclusion, RLs and their precursors released by bacteria can both be perceived by plants but through distinct mechanisms.

SignificanceActivation of plant innate immunity relies on the perception of microorganisms through self and nonself elicitors. Rhamnolipids and their precursor HAAs are exoproducts produced by beneficial and pathogenic bacteria. They are involved in bacterial surface dissemination and biofilm development. As these compounds are released in the extracellular milieu, they have the potential to be perceived by the plant immune system. Our work shows that both compounds independently activate plant immunity. We demonstrate that HAAs are perceived by the receptor protein kinase LORE. By contrast, rhamnolipids are not senses by LORE but activate a non-canonical immune response affected by the sphingolipid composition of the plant plasma membrane. Thus, plants are able to sense bacterial molecules as well as their direct precursors to trigger a distinct immune response.
]]></description>
<dc:creator>Schellenberger, R.</dc:creator>
<dc:creator>Crouzet, J.</dc:creator>
<dc:creator>Nickzad, A.</dc:creator>
<dc:creator>Kutschera, A.</dc:creator>
<dc:creator>Gerster, T.</dc:creator>
<dc:creator>Borie, N.</dc:creator>
<dc:creator>Dawid, C.</dc:creator>
<dc:creator>Cloutier, M.</dc:creator>
<dc:creator>Villaume, S.</dc:creator>
<dc:creator>Dhondt-Cordelier, S.</dc:creator>
<dc:creator>Hubert, J.</dc:creator>
<dc:creator>Cordelier, S.</dc:creator>
<dc:creator>Mazeyrat-Gourbeyre, F.</dc:creator>
<dc:creator>Schmid, C.</dc:creator>
<dc:creator>Ongena, M.</dc:creator>
<dc:creator>Renault, J.-H.</dc:creator>
<dc:creator>Haudrechy, A.</dc:creator>
<dc:creator>Hofmann, T.</dc:creator>
<dc:creator>Baillieul, F.</dc:creator>
<dc:creator>Clement, C.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Gauthier, C.</dc:creator>
<dc:creator>Deziel, E.</dc:creator>
<dc:creator>Ranf, S.</dc:creator>
<dc:creator>Dorey, S.</dc:creator>
<dc:date>2020-12-20</dc:date>
<dc:identifier>doi:10.1101/2020.12.18.423392</dc:identifier>
<dc:title><![CDATA[Rhamnolipids and their 3-(3-hydroxyalkanoyloxy)alkanoic acid precursors activate Arabidopsis innate immunity through two independent mechanisms]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-12-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.12.21.423810v1?rss=1">
<title>
<![CDATA[
Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.12.21.423810v1?rss=1"
</link>
<description><![CDATA[
Plants utilise intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors to detect pathogen effectors and activate local and systemic defence. NRG1 and ADR1 "helper" NLRs (RNLs), cooperate with enhanced disease susceptibility 1 (EDS1), senescence-associated gene 101 (SAG101) and phytoalexin-deficient 4 (PAD4) lipase-like proteins to mediate signalling from TIR domain NLR receptors (TNLs). However, the mechanism of RNL/EDS1-family protein cooperation is poorly understood. Here, we provide genetic and molecular evidence for exclusive EDS1/SAG101/NRG1 and EDS1/PAD4/ADR1 co-functions in TNL immunity. Using immunoprecipitation and mass spectrometry, we show effector recognition-dependent association of NRG1 with EDS1 and SAG101, but not PAD4. An EDS1-SAG101 complex associates with NRG1, and EDS1-PAD4 associates with ADR1, only in an immune-activated state. NRG1 requires an intact nucleotide-binding P-loop motif, and EDS1 a functional EP domain and its partner SAG101, for induced association and immunity. Thus, two distinct modules (NRG1/EDS1/SAG101 and ADR1/EDS1/PAD4) are required to execute TNL receptor defence signalling.
]]></description>
<dc:creator>Sun, X.</dc:creator>
<dc:creator>Lapin, D.</dc:creator>
<dc:creator>Feehan, J. M.</dc:creator>
<dc:creator>Stolze, S. C.</dc:creator>
<dc:creator>Kramer, K.</dc:creator>
<dc:creator>Dongus, J. A.</dc:creator>
<dc:creator>Rzemieniewski, J.</dc:creator>
<dc:creator>Blanvillain-Baufume, S.</dc:creator>
<dc:creator>Harzen, A.</dc:creator>
<dc:creator>Bautor, J.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Finkemeier, I.</dc:creator>
<dc:creator>Nakagami, H.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:creator>Parker, J. E.</dc:creator>
<dc:date>2020-12-22</dc:date>
<dc:identifier>doi:10.1101/2020.12.21.423810</dc:identifier>
<dc:title><![CDATA[Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-12-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.12.28.423414v1?rss=1">
<title>
<![CDATA[
The phagocytosis oxidase/Bem1p (PB1) domain-containing protein PB1CP negatively regulates the NADPH oxidase RBOHD in plant immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.12.28.423414v1?rss=1"
</link>
<description><![CDATA[
O_LIPerception of pathogen-associated molecular patterns (PAMPs) by surface-localized pattern-recognition receptors activates RESPIRATORY BURST OXIDASE HOMOLOG D (RBOHD) through direct phosphorylation by BOTRYTIS-INDUCED KINASE 1 (BIK1) and induces the production of reactive oxygen species (ROS). ROS have direct antimicrobial properties but also serve as signaling molecules to activate additional defense responses such as stomatal closure. RBOHD activity must be tightly controlled to avoid the detrimental effects of ROS, but little is known about RBOHD downregulation.
C_LIO_LITo better understand the regulation of RBOHD, we used co-immunoprecipitation of RBOHD coupled with mass spectrometry analysis to identify RBOHD-associated proteins.
C_LIO_LIAmong RBOHD-associated proteins, we identified PHAGOCYTOSIS OXIDASE/ BEM1P (PB1) DOMAIN-CONTAINING PROTEIN (PB1CP). We found that PB1CP negatively regulates RBOHD and the resistance against the fungal pathogen Colletotrichum higginsianum. PB1CP directly interacts with RBOHD in vitro, and PAMP treatment increases the interaction in vivo. PB1CP is localized at the cell periphery and in cytoplasm, but PAMP treatment induces PB1CP relocalization to small endomembrane compartments. PB1CP overexpression reduces plasma membrane localization of RBOHD, suggesting that PB1CP down-regulates RBOHD function by relocalizing it away from the plasma membrane.
C_LIO_LIWe reveal a novel negative regulation mechanism of ROS production through the relocalization of RBOHD by PB1CP.
C_LI
]]></description>
<dc:creator>Goto, Y.</dc:creator>
<dc:creator>Maki, N.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Kadota, Y.</dc:creator>
<dc:creator>Shirasu, K.</dc:creator>
<dc:date>2020-12-29</dc:date>
<dc:identifier>doi:10.1101/2020.12.28.423414</dc:identifier>
<dc:title><![CDATA[The phagocytosis oxidase/Bem1p (PB1) domain-containing protein PB1CP negatively regulates the NADPH oxidase RBOHD in plant immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-12-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2020.12.29.424692v1?rss=1">
<title>
<![CDATA[
Allelic variants of the NLR protein Rpi-chc1 differentially recognise members of the Phytophthora infestans PexRD12/31 effector superfamily through the leucine-rich repeat domain 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2020.12.29.424692v1?rss=1"
</link>
<description><![CDATA[
O_LIPhytophthora infestans is a pathogenic oomycete that causes the infamous potato late blight disease. Resistance (R) genes from diverse Solanum species encode intracellular receptors that recognize P. infestans RXLR effector proteins and provide effective defence responses. To deploy these R genes in a durable fashion in agriculture, we need to understand the mechanism of effector recognition and the way the pathogen evades recognition.
C_LIO_LIWe cloned sixteen allelic variants of the Rpi-chc1 gene from Solanum chacoense and other Solanum species, and identified the cognate P. infestans RXLR effectors. These tools were used to study receptor-ligand interactions and co-evolution.
C_LIO_LIFunctional and non-functional alleles of Rpi-chc1 encode Coiled-Coil-Nucleotide Binding-Leucine-Rich-Repeat (CNL) proteins. Rpi-chc1.1 recognised multiple PexRD12 (AVRchc1.1) proteins while Rpi-chc1.2 recognised multiple PexRD31 (AVRchc1.2) proteins, both from the PexRD12/31 superfamily. Domain swaps between Rpi-chc1.1 and Rpi-chc1.2 revealed that overlapping subdomains in the LRR were responsible for the difference in effector recognition.
C_LIO_LIThis study showed that Rpi-chc1.1 and Rpi-chc1.2, evolved to recognize distinct members of the same PexRD12/31 effector family via the LRR domain. The biased distribution of polymorphisms suggests that exchange of LRRs during host-pathogen co-evolution can lead to novel recognition specificities. These insights will help future strategies to breed for durable resistant varieties.
C_LI
]]></description>
<dc:creator>Monino Lopez, D.</dc:creator>
<dc:creator>Nijenhuis, M.</dc:creator>
<dc:creator>Kodde, L.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Salehian, H.</dc:creator>
<dc:creator>Schenstnyi, K.</dc:creator>
<dc:creator>Stam, R.</dc:creator>
<dc:creator>Lokossou, A.</dc:creator>
<dc:creator>Abd'el Haliem, A.</dc:creator>
<dc:creator>Visser, R.</dc:creator>
<dc:creator>Vossen, J.</dc:creator>
<dc:date>2020-12-30</dc:date>
<dc:identifier>doi:10.1101/2020.12.29.424692</dc:identifier>
<dc:title><![CDATA[Allelic variants of the NLR protein Rpi-chc1 differentially recognise members of the Phytophthora infestans PexRD12/31 effector superfamily through the leucine-rich repeat domain]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2020-12-30</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.01.19.427293v1?rss=1">
<title>
<![CDATA[
A conserved regulatory module regulates receptor kinase signaling in immunity and development 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.01.19.427293v1?rss=1"
</link>
<description><![CDATA[
Ligand recognition by cell-surface receptors underlies development and immunity in both animals and plants. Modulating receptor signaling is critical for appropriate cellular responses but the mechanisms ensuring this are poorly understood. Here, we show that signaling by plant receptors for pathogen-associated molecular patterns (PAMPs) in immunity and CLAVATA3/EMBRYO SURROUNDING REGION-RELATED peptides (CLEp) in development employ a similar regulatory module. In the absence of ligand, signaling is dampened through association with specific type-2C protein phosphatases (PP2Cs). Upon activation, PAMP and CLEp receptors phosphorylate divergent cytosolic kinases, which, in turn, phosphorylate the phosphatases, thereby promoting their release from the receptor complexes. Our work reveals a regulatory circuit shared between immune and developmental receptor signaling, which may have broader important implications for plant receptor kinase-mediated signaling in general.
]]></description>
<dc:creator>DeFalco, T. A.</dc:creator>
<dc:creator>Anne, P.</dc:creator>
<dc:creator>James, S. R.</dc:creator>
<dc:creator>Willoughby, A.</dc:creator>
<dc:creator>Johanndrees, O.</dc:creator>
<dc:creator>Genolet, Y.</dc:creator>
<dc:creator>Pullen, A.-M.</dc:creator>
<dc:creator>zipfel, c.</dc:creator>
<dc:creator>Hardtke, C.</dc:creator>
<dc:creator>Nimchuk, Z. L.</dc:creator>
<dc:date>2021-01-20</dc:date>
<dc:identifier>doi:10.1101/2021.01.19.427293</dc:identifier>
<dc:title><![CDATA[A conserved regulatory module regulates receptor kinase signaling in immunity and development]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-01-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.01.22.427732v1?rss=1">
<title>
<![CDATA[
The Arabidopsis immune receptor EFR increases resistance to the bacterial pathogens Xanthomonas and Xylella in transgenic sweet orange 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.01.22.427732v1?rss=1"
</link>
<description><![CDATA[
Plants employ cell surface receptors to recognize pathogen (or microbe)-associated molecular patterns (PAMPs/MAMPs), which are crucial for immune system activation. The well-studied Arabidopsis thaliana ELONGATION FACTOR-TU RECEPTOR (EFR) recognizes the conserved bacterial PAMP EF-Tu, and the derived peptides elf18 and elf26. The interfamily transfer of EFR has been shown to increase disease resistance in several crops, such as tomato, rice, wheat, and potato. Here, we generated sweet orange (Citrus sinensis) transgenic lines expressing EFR to test if it would confer broad-spectrum resistance against two important citrus bacterial diseases: citrus canker and citrus variegated chlorosis (CVC). Independent EFR transgenic lines gained responsiveness to elf18 and elf26 peptides from Xanthomonas citri and Xylella fastidiosa, as measured by reactive oxygen species (ROS) production, mitogen-activated protein kinase (MAPK) activation and defense gene expression. Consistently, infection assays showed that Citrus-EFR transgenic plants were more resistant to citrus canker and CVC. Our results show that the EFR immune receptor can improve plant immunity in a perennial crop against bacterial pathogens, opening perspectives to engineer durable broad-spectrum disease resistance under field conditions.
]]></description>
<dc:creator>Mitre, L. K.</dc:creator>
<dc:creator>Teixeira-Silva, N. S.</dc:creator>
<dc:creator>Rybak, K.</dc:creator>
<dc:creator>Magalhaes, D. M.</dc:creator>
<dc:creator>de Souza-Neto, R. R.</dc:creator>
<dc:creator>Robatzek, S.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>De Souza, A. A.</dc:creator>
<dc:date>2021-01-22</dc:date>
<dc:identifier>doi:10.1101/2021.01.22.427732</dc:identifier>
<dc:title><![CDATA[The Arabidopsis immune receptor EFR increases resistance to the bacterial pathogens Xanthomonas and Xylella in transgenic sweet orange]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-01-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.01.22.427734v1?rss=1">
<title>
<![CDATA[
The Arabidopsis pattern recognition receptor EFR enhances fire blight resistance in apple 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.01.22.427734v1?rss=1"
</link>
<description><![CDATA[
Fire blight disease, caused by the bacterium Erwinia amylovora (E. amylovora), is responsible for substantial losses in cultivated apple worldwide. An important mechanism of plant immunity is based on the recognition of conserved microbial molecules, named pathogen- or microbe-associated molecular patterns (PAMPs or MAMPs), through pattern recognition receptors (PRRs), leading to pattern-triggered immunity (PTI). The interspecies transfer of PRRs represents a promising strategy to engineer broad spectrum and durable disease resistance in crops. EFR, the Arabidopsis thaliana PRR for the PAMP elf18 derived from the elongation factor thermal unstable (EF-Tu) proved to be effective in improving bacterial resistance when expressed into Solanaceae and other plant species. In this study, we tested whether EFR can affect the interaction of apple with E. amylovora by its ectopic expression in the susceptible apple rootstock M.26. Stable EFR expression led to the activation of PAMP-triggered immune response in apple leaves upon treatment with supernatant of E. amylovora, as measured by production of reactive oxygen species and the induction of known defense genes. The amount of tissue necrosis associated with E. amylovora infection was significantly reduced in the EFR transgenic rootstock compared to the wild-type. Our results show that the expression of EFR in apple rootstock may be a valuable biotechnology strategy to improve the resistance of apple to fire blight.
]]></description>
<dc:creator>Piazza, S.</dc:creator>
<dc:creator>Campa, M.</dc:creator>
<dc:creator>Pompili, V.</dc:creator>
<dc:creator>Costa, L. D.</dc:creator>
<dc:creator>Salvagnin, U.</dc:creator>
<dc:creator>Nekrasov, V.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Malnoy, M.</dc:creator>
<dc:date>2021-01-22</dc:date>
<dc:identifier>doi:10.1101/2021.01.22.427734</dc:identifier>
<dc:title><![CDATA[The Arabidopsis pattern recognition receptor EFR enhances fire blight resistance in apple]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-01-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.01.24.427197v1?rss=1">
<title>
<![CDATA[
Genome evolution of a non-parasitic secondary heterotroph, the diatom Nitzschia putrida 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.01.24.427197v1?rss=1"
</link>
<description><![CDATA[
Secondary loss of photosynthesis is observed across almost all plastid-bearing branches of the eukaryotic tree of life. However, genome-based insights into the transition from a phototroph into a secondary heterotroph have so far only been revealed for parasitic species. Free-living organisms can yield unique insights into the evolutionary consequence of the loss of photosynthesis, as the parasitic lifestyle requires specific adaptations to host environments. Here we report on the diploid genome of the free-living diatom Nitzschia putrida (35 Mbp), a non-photosynthetic osmotroph whose photosynthetic relatives contribute ca. 40% of net oceanic primary production. Comparative analyses with photosynthetic diatoms revealed that a combination of genes loss, the horizontal acquisition of genes involved in organic carbon degradation, a unique secretome and the rapid divergence of conserved gene families involved in cell wall and extracellular metabolism appear to have facilitated the lifestyle of a non-parasitic, free-living secondary heterotroph.
]]></description>
<dc:creator>Kamikawa, R.</dc:creator>
<dc:creator>Mochizuki, T.</dc:creator>
<dc:creator>Sakamoto, M.</dc:creator>
<dc:creator>Tanizawa, Y.</dc:creator>
<dc:creator>Nakayama, T.</dc:creator>
<dc:creator>Onuma, R.</dc:creator>
<dc:creator>Cenci, U.</dc:creator>
<dc:creator>Moog, D.</dc:creator>
<dc:creator>Speak, S.</dc:creator>
<dc:creator>Sarkozi, K.</dc:creator>
<dc:creator>Toseland, A.</dc:creator>
<dc:creator>van Oosterhout, C.</dc:creator>
<dc:creator>Oyama, K.</dc:creator>
<dc:creator>Kato, M.</dc:creator>
<dc:creator>Kume, K.</dc:creator>
<dc:creator>Kayama, M.</dc:creator>
<dc:creator>Azuma, T.</dc:creator>
<dc:creator>Ishii, K.-i.</dc:creator>
<dc:creator>Miyashita, H.</dc:creator>
<dc:creator>Henrissat, B.</dc:creator>
<dc:creator>Lombard, V.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Kashiyama, Y.</dc:creator>
<dc:creator>Mayama, S.</dc:creator>
<dc:creator>Miyagishima, S.-y.</dc:creator>
<dc:creator>Tanifuji, G.</dc:creator>
<dc:creator>Mock, T.</dc:creator>
<dc:creator>Nakamura, Y.</dc:creator>
<dc:date>2021-01-24</dc:date>
<dc:identifier>doi:10.1101/2021.01.24.427197</dc:identifier>
<dc:title><![CDATA[Genome evolution of a non-parasitic secondary heterotroph, the diatom Nitzschia putrida]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-01-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.01.26.428286v1?rss=1">
<title>
<![CDATA[
Two NLR immune receptors acquired high-affinity binding to a fungal effector through convergent evolution of their integrated domain 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.01.26.428286v1?rss=1"
</link>
<description><![CDATA[
A subset of plant NLR immune receptors carry unconventional integrated domains in addition to their canonical domain architecture. One example is rice Pik-1 that comprises an integrated heavy metal-associated (HMA) domain. Here, we reconstructed the evolutionary history of Pik-1 and its NLR partner, Pik-2, and tested hypotheses about adaptive evolution of the HMA domain. Phylogenetic analyses revealed that the HMA domain integrated into Pik-1 before Oryzinae speciation over 15 million years ago and has been under diversifying selection. Ancestral sequence reconstruction coupled with functional studies showed that two Pik-1 allelic variants independently evolved from a weakly binding ancestral state to high-affinity binding of the blast fungus effector AVR-PikD. We conclude that for most of its evolutionary history the Pik-1 HMA domain did not sense AVR-PikD, and that different Pik-1 receptors have recently evolved through distinct biochemical paths to produce similar phenotypic outcomes. These findings highlight the dynamic nature of the evolutionary mechanisms underpinning NLR adaptation to plant pathogens.
]]></description>
<dc:creator>Bialas, A.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Stevenson, C. E. M.</dc:creator>
<dc:creator>Lawson, D. M.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Kellner, R.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2021-01-27</dc:date>
<dc:identifier>doi:10.1101/2021.01.26.428286</dc:identifier>
<dc:title><![CDATA[Two NLR immune receptors acquired high-affinity binding to a fungal effector through convergent evolution of their integrated domain]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-01-27</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.01.28.428637v1?rss=1">
<title>
<![CDATA[
A novel allele in the Arabidopsis thaliana MACPF protein CAD1 results in deregulated immune signaling 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.01.28.428637v1?rss=1"
</link>
<description><![CDATA[
Immune recognition in plants is governed by two major classes of receptors: pattern recognition receptors (PRRs) and nucleotide-binding leucine-rich repeat receptors (NLRs). Located at the cell surface, PRRs bind extracellular ligands originating from microbes (indicative of  non-self) or damaged plant cells (indicative of  infected-self), and trigger signaling cascades to protect against infection. Located intracellularly, NLRs sense pathogen-induced physiological changes and trigger localized cell death and systemic resistance. Immune responses are under tight regulation in order to maintain homeostasis and promote plant health. In a forward-genetic screen to identify regulators of PRR-mediated immune signaling, we identified a novel allele of the membrane-attack complex and perforin (MACPF)-motif containing protein CONSTITUTIVE ACTIVE DEFENSE 1 (CAD1) resulting from a missense mutation in a conserved N-terminal cysteine. We show that cad1-5 mutants display deregulated immune signaling and symptoms of autoimmunity dependent on the lipase-like protein ENHANCED DISEASE SUSCEPTIBILITY1 (EDS1), suggesting that CAD1 integrity is monitored by the plant immune system. We further demonstrate that CAD1 localizes to both the cytosol and plasma membrane using confocal microscopy and subcellular fractionation. Our results offer new insights into immune homeostasis and provide tools to further decipher the intriguing role of MACPF proteins in plants.
]]></description>
<dc:creator>Holmes, D. R.</dc:creator>
<dc:creator>Bredow, M.</dc:creator>
<dc:creator>Thor, K.</dc:creator>
<dc:creator>Pascetta, S. A.</dc:creator>
<dc:creator>Sementchoukova, I.</dc:creator>
<dc:creator>Siegel, K. R.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Monaghan, J.</dc:creator>
<dc:date>2021-01-28</dc:date>
<dc:identifier>doi:10.1101/2021.01.28.428637</dc:identifier>
<dc:title><![CDATA[A novel allele in the Arabidopsis thaliana MACPF protein CAD1 results in deregulated immune signaling]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-01-28</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.01.28.428596v1?rss=1">
<title>
<![CDATA[
A hetero-oligomeric remorin-receptor complex regulates plant development 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.01.28.428596v1?rss=1"
</link>
<description><![CDATA[
Plant growth and development are modulated by both biotic and abiotic stress. Increasing evidence suggests that cellular integration of the corresponding signals occurs within preformed hubs at the plasma membrane called nanodomains. These membrane sub-compartments are organized by multivalent molecular scaffold proteins, such as remorins. Here, we demonstrate that Group 1 remorins form a hetero-oligomeric complex at the plasma membrane. While these remorins are functionally redundant for some pathways their multivalency also allows the recruitment of specific interaction partners. One of them, the receptor-like kinase REMORIN-INTERACTING RECEPTOR 1 (RIR1), that acts redundantly with the closely related receptor NILR2, is specifically recruited by REM1.2 in a phosphorylation-dependent manner. Overlapping developmental phenotypes suggest that the REM/RIR complex regulates key developmental pathways.
]]></description>
<dc:creator>Abel, N. B.</dc:creator>
<dc:creator>Buschle, C. A.</dc:creator>
<dc:creator>Hernandez-Ryes, C.</dc:creator>
<dc:creator>Burkart, S. S.</dc:creator>
<dc:creator>Deroubaix, A.-F.</dc:creator>
<dc:creator>Mergner, J.</dc:creator>
<dc:creator>Gronnier, J.</dc:creator>
<dc:creator>Jarsch, I. K.</dc:creator>
<dc:creator>Folgmann, J.</dc:creator>
<dc:creator>Braun, K. H.</dc:creator>
<dc:creator>Bayer, E.</dc:creator>
<dc:creator>Germain, V.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Kemmerling, B.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Kuester, B.</dc:creator>
<dc:creator>Mongrand, S.</dc:creator>
<dc:creator>Marin, M.</dc:creator>
<dc:creator>Ott, T.</dc:creator>
<dc:date>2021-01-29</dc:date>
<dc:identifier>doi:10.1101/2021.01.28.428596</dc:identifier>
<dc:title><![CDATA[A hetero-oligomeric remorin-receptor complex regulates plant development]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-01-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.02.03.429184v1?rss=1">
<title>
<![CDATA[
Plant pathogens convergently evolved to counteract redundant nodes of an NLR immune receptor network 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.02.03.429184v1?rss=1"
</link>
<description><![CDATA[
In plants, NLR (nucleotide-binding domain and leucine-rich repeat-containing) proteins can form receptor networks to confer hypersensitive cell death and innate immunity. One class of NLRs, known as NRCs (NLR required for cell death), are central nodes in a complex network that protects against multiple pathogens and comprises up to half of the NLRome of solanaceous plants. Given the prevalence of this NLR network, we hypothesized that pathogens convergently evolved to secrete effectors that target NRC activities. To test this, we screened a library of 167 bacterial, oomycete, nematode and aphid effectors for their capacity to suppress the cell death response triggered by the NRC-dependent disease resistance proteins Prf and Rpi-blb2. Among five of the identified suppressors, one cyst nematode protein and one oomycete protein suppress the activity of autoimmune mutants of NRC2 and NRC3, but not NRC4, indicating that they specifically counteract a subset of NRC proteins independently of their sensor NLR partners. Whereas the cyst nematode effector SPRYSEC15 binds the nucleotide-binding domain of NRC2 and NRC3, the oomycete effector AVRcap1b suppresses the response of these NRCs via the membrane trafficking-associated protein NbTOL9a (Target of Myb 1-like protein 9a). We conclude that plant pathogens have evolved to counteract central nodes of the NRC immune receptor network through different mechanisms. Coevolution with pathogen effectors may have driven NRC diversification into functionally redundant nodes in a massively expanded NLR network.
]]></description>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Upson, J.</dc:creator>
<dc:creator>Vergara Cruces, A.</dc:creator>
<dc:creator>Xie, R.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Menke, F. L.</dc:creator>
<dc:creator>Mugford, S. T.</dc:creator>
<dc:creator>MacLean, D. T.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Hogenhout, S. A.</dc:creator>
<dc:creator>Goverse, A.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Wu, C.-h.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2021-02-03</dc:date>
<dc:identifier>doi:10.1101/2021.02.03.429184</dc:identifier>
<dc:title><![CDATA[Plant pathogens convergently evolved to counteract redundant nodes of an NLR immune receptor network]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-02-03</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.02.08.430144v1?rss=1">
<title>
<![CDATA[
Biophysical and proteomic analyses suggest functions of Pseudomonas syringae pv tomato DC3000 extracellular vesicles in bacterial growth during plant infection 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.02.08.430144v1?rss=1"
</link>
<description><![CDATA[
Vesiculation is a process employed by Gram-negative bacteria to release extracellular vesicles (EVs) into the environment. Bacterial EVs contain molecular cargo from the donor bacterium and play important roles in bacterial survival and growth. Here, we describe EV production in plant-pathogenic Pseudomonas syringae pv. tomato DC3000 (Pto DC3000), the causal agent of bacterial speck disease. Cultured Pto DC3000 exhibited EV structures both on the cell surface and in the vicinity of bacterial cells, observed as outer membrane vesicle (OMV) release. We used in-solution trypsin digestion coupled to mass spectrometry to identify 369 proteins enriched in EVs recovered from cultured Pto DC3000. The predicted localization profile of EV proteins supports the production of EVs also in the form of outer-inner-membrane vesicles (OIMVs). EV production varied slightly between bacterial lifestyles and also occurred in planta. The potential contribution of EVs to Pto DC3000 plant infection was assessed using plant treatments and bioinformatic analysis of the EV-enriched proteins. While these results identify immunogenic activities of the EVs, they also point at roles for EVs in bacterial defences and nutrient acquisition by Pto DC3000.
]]></description>
<dc:creator>Janda, M.</dc:creator>
<dc:creator>Ludwig, C.</dc:creator>
<dc:creator>Rybak, K.</dc:creator>
<dc:creator>Meng, C.</dc:creator>
<dc:creator>Stigliano, E.</dc:creator>
<dc:creator>Botzenhardt, L.</dc:creator>
<dc:creator>Szulc, B.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Malone, J. G.</dc:creator>
<dc:creator>Brachmann, A.</dc:creator>
<dc:creator>Klingl, A.</dc:creator>
<dc:creator>Robatzek, S.</dc:creator>
<dc:date>2021-02-08</dc:date>
<dc:identifier>doi:10.1101/2021.02.08.430144</dc:identifier>
<dc:title><![CDATA[Biophysical and proteomic analyses suggest functions of Pseudomonas syringae pv tomato DC3000 extracellular vesicles in bacterial growth during plant infection]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-02-08</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.02.15.430920v1?rss=1">
<title>
<![CDATA[
Parasite co-opts a ubiquitin receptor to induce a plethora of developmental changes 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.02.15.430920v1?rss=1"
</link>
<description><![CDATA[
Obligate parasites can induce complex and substantial phenotypic changes in their hosts in ways that favour their transmission to other trophic levels. However, mechanisms underlying these changes remain largely unknown. Here, we demonstrate how SAP05 protein effectors from insect-vectored plant pathogenic phytoplasmas take control of several plant developmental processes to simultaneously prolong host lifespan and induce witchs broom-like proliferations of leaf and sterile shoots, organs colonized by phytoplasmas and vectors. SAP05 acts by mediating the concurrent degradation of SPL and GATA developmental regulators via a process that uniquely relies on hijacking the plant ubiquitin receptor RPN10 independently of substrate lysine ubiquitination. RPN10 is highly conserved among eukaryotes, but SAP05 does not bind insect vector RPN10. A two-amino-acid substitution within plant RPN10 generates a functional variant that is resistant to SAP05 activities. Therefore, one effector protein enables obligate parasitic phytoplasmas to induce a plethora of developmental phenotypes in their hosts.
]]></description>
<dc:creator>Huang, W.</dc:creator>
<dc:creator>MacLean, A.</dc:creator>
<dc:creator>Sugio, A.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Busscher, M.</dc:creator>
<dc:creator>Cho, S.-T.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Kuo, C.-H.</dc:creator>
<dc:creator>Immink, R. G. H.</dc:creator>
<dc:creator>Hogenhout, S. A.</dc:creator>
<dc:date>2021-02-15</dc:date>
<dc:identifier>doi:10.1101/2021.02.15.430920</dc:identifier>
<dc:title><![CDATA[Parasite co-opts a ubiquitin receptor to induce a plethora of developmental changes]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-02-15</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.03.15.435478v1?rss=1">
<title>
<![CDATA[
A single amino acid polymorphism in a conserved effector of the multihost blast fungus pathogen expands host-target binding spectrum 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.03.15.435478v1?rss=1"
</link>
<description><![CDATA[
Accelerated gene evolution is a hallmark of pathogen adaptation and specialization following host-jumps. However, the molecular processes associated with adaptive evolution between host-specific lineages of a multihost plant pathogen remain poorly understood. In the blast fungus Magnaporthe oryzae (Syn. Pyricularia oryzae), host specialization on different grass hosts is generally associated with dynamic patterns of gain and loss of virulence effector genes that tend to define the distinct genetic lineages of this pathogen. Here, we unravelled the biochemical and structural basis of adaptive evolution of APikL2, an exceptionally conserved paralog of the well-studied rice-lineage specific effector AVR-Pik. Whereas AVR-Pik and other members of the six-gene AVR-Pik family show specific patterns of presence/absence polymorphisms between grassspecific lineages of M. oryzae, APikL2 stands out by being ubiquitously present in all blast fungus lineages from 13 different host species. Using biochemical, biophysical and structural biology methods, we show that a single aspartate to asparagine polymorphism expands the binding spectrum of APikL2 to host proteins of the heavy-metal associated (HMA) domain family. This mutation maps to one of the APikL2-HMA binding interfaces and contributes to an altered hydrogen-bonding network. By combining phylogenetic ancestral reconstruction with an analysis of the structural consequences of allelic diversification, we revealed a common mechanism of effector specialization in the AVR-Pik/APikL2 family that involves two major HMA-binding interfaces. Together, our findings provide a detailed molecular evolution and structural biology framework for diversification and adaptation of a fungal pathogen effector family following host-jumps.
]]></description>
<dc:creator>Bentham, A. R.</dc:creator>
<dc:creator>Petit-Houdenot, Y.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Chuma, I.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:date>2021-03-16</dc:date>
<dc:identifier>doi:10.1101/2021.03.15.435478</dc:identifier>
<dc:title><![CDATA[A single amino acid polymorphism in a conserved effector of the multihost blast fungus pathogen expands host-target binding spectrum]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-03-16</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.03.15.435521v1?rss=1">
<title>
<![CDATA[
Dynamic accumulation of a helper NLR at the plant-pathogen interface underpins pathogen recognition 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.03.15.435521v1?rss=1"
</link>
<description><![CDATA[
Plants employ sensor-helper pairs of NLR immune receptors to recognize pathogen effectors and activate immune responses. Yet the subcellular localization of NLRs pre- and post-activation during pathogen infection remains poorly known. Here we show that NRC4, from the  NRC solanaceous helper NLR family, undergoes dynamic changes in subcellular localization by shuttling to and from the plant-pathogen haustorium interface established during infection by the Irish potato famine pathogen Phytophthora infestans. Specifically, prior to activation, NRC4 accumulates at the extra-haustorial membrane (EHM), presumably to mediate response to perihaustorial effectors, that are recognized by NRC4-dependent sensor NLRs. However not all NLRs accumulate at the EHM, as the closely related helper NRC2, and the distantly related ZAR1, did not accumulate at the EHM. NRC4 required an intact N-terminal coiled coil domain to accumulate at the EHM, whereas the functionally conserved MADA motif implicated in cell death activation and membrane insertion was dispensable for this process. Strikingly, a constitutively autoactive NRC4 mutant did not accumulate at the EHM and showed punctate distribution that mainly associated with the plasma membrane, suggesting that post-activation, NRC4 probably undergoes a conformation switch to form clusters that do not preferentially associate with the EHM. When NRC4 is activated by a sensor NLR during infection however, NRC4 formed puncta mainly at the EHM and to a lesser extent at the plasma membrane. We conclude that following activation at the EHM, NRC4 may spread to other cellular membranes from its primary site of activation to trigger immune responses.

Significance statementPlant NLR immune receptors function as intracellular sensors of pathogen virulence factors known as effectors. In resting state, NLRs localize to subcellular sites where the effectors they sense operate. However, the extent to which NLRs alter their subcellular distribution during infection remains elusive. We describe dynamic changes in spatiotemporal localization of an NLR protein in infected plant cells. Specifically, the NLR protein accumulates at the newly synthesized plant-pathogen interface membrane, where the corresponding effectors are deployed. Following immune recognition, the activated receptor re-organizes to form punctate structures that target the cell periphery. We propose that NLRs are not necessarily stationary immune receptors, but instead may spread to other cellular membranes from the primary site of activation to boost immune responses.
]]></description>
<dc:creator>Duggan, C.</dc:creator>
<dc:creator>Moratto, E.</dc:creator>
<dc:creator>Savage, Z.</dc:creator>
<dc:creator>Hamilton, E.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Leary, A. Y.</dc:creator>
<dc:creator>Tumtas, Y.</dc:creator>
<dc:creator>Rothery, S.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:date>2021-03-16</dc:date>
<dc:identifier>doi:10.1101/2021.03.15.435521</dc:identifier>
<dc:title><![CDATA[Dynamic accumulation of a helper NLR at the plant-pathogen interface underpins pathogen recognition]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-03-16</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.03.29.436918v1?rss=1">
<title>
<![CDATA[
The Arabidopsis WRR4A and WRR4B paralogous NLR proteins both confer recognition of multiple Albugo candida effectors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.03.29.436918v1?rss=1"
</link>
<description><![CDATA[
The oomycete Albugo candida causes white blister rust, an important disease of Brassica crops. Distinct races of A. candida are defined by their specificity for infecting different host species.

The White Rust Resistance 4 (WRR4) locus in Col-0 accession of Arabidopsis thaliana contains three genes that encode TIR-NLR resistance proteins. The Col-0 alleles of WRR4A and WRR4B confer resistance to at least four A. candida races (2, 7 and 9 from B. juncea, B. rapa and B. oleracea, respectively, and Race 4 from Capsella bursa-pastoris). Resistance mediated by both paralogs can be overcome by Col-0-virulent isolates of Race 4.

After comparing repertoires of candidate effectors in resisted and resistance-breaking strains, we used transient co-expression in tobacco or Arabidopsis to identify effectors recognized by WRR4A and WRR4B. A library of CCG effectors from four A. candida races was screened for WRR4A- or WRR4B- dependent elicitation of hypersensitive response (HR). These CCG genes were validated for WRR-dependent HR by bombardment assays in wild type Col-0, wrr4A or wrr4B mutants.

Our analysis revealed eight WRR4A-recognized CCGs and four WRR4B-recognized CCGs. Remarkably, the N-terminal region of 100 amino acids after the secretion signal is sufficient for WRR4A recognition of these eight recognized effectors. This multiple recognition capacity potentially explains the broad-spectrum resistance to many A. candida races conferred by WRR4 paralogs.
]]></description>
<dc:creator>Redkar, A.</dc:creator>
<dc:creator>Cevik, V.</dc:creator>
<dc:creator>Bailey, K.</dc:creator>
<dc:creator>Furzer, O. J.</dc:creator>
<dc:creator>Fairhead, S.</dc:creator>
<dc:creator>Borhan, M. H.</dc:creator>
<dc:creator>Holub, E. B.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:date>2021-03-29</dc:date>
<dc:identifier>doi:10.1101/2021.03.29.436918</dc:identifier>
<dc:title><![CDATA[The Arabidopsis WRR4A and WRR4B paralogous NLR proteins both confer recognition of multiple Albugo candida effectors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-03-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.03.29.437041v1?rss=1">
<title>
<![CDATA[
An improved assembly of the Albugo candida Ac2V genome reveals the expansion of the "CCG" class of effectors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.03.29.437041v1?rss=1"
</link>
<description><![CDATA[
Albugo candida is an obligate oomycete pathogen that infects many plants in the Brassicaceae family. We re-sequenced the genome of isolate Ac2V using PacBio long reads and constructed an assembly augmented by Illumina reads. The Ac2VPB genome assembly is 10% larger and more contiguous compared to a previous version. Our annotation of the new assembly, aided by RNASeq information, revealed a dramatic 250% expansion (40 to 110) in the CHxC effector class, which we redefined as "CCG" based on motif analysis. This class of effectors consist of arrays of phylogenetically related paralogs residing in gene sparse regions, and shows signatures of positive selection and presence/absence polymorphism. This work provides a resource that allows the dissection of the genomic components underlying A. candida adaptation and particularly the role of CCG effectors in virulence and avirulence on different hosts.
]]></description>
<dc:creator>Furzer, O. J.</dc:creator>
<dc:creator>Cevik, V.</dc:creator>
<dc:creator>Fairhead, S.</dc:creator>
<dc:creator>Bailey, K.</dc:creator>
<dc:creator>Redkar, A.</dc:creator>
<dc:creator>Schudoma, C.</dc:creator>
<dc:creator>MacLean, D.</dc:creator>
<dc:creator>Holub, E. B.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:date>2021-03-29</dc:date>
<dc:identifier>doi:10.1101/2021.03.29.437041</dc:identifier>
<dc:title><![CDATA[An improved assembly of the Albugo candida Ac2V genome reveals the expansion of the "CCG" class of effectors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-03-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.03.29.437434v1?rss=1">
<title>
<![CDATA[
Evolutionary trade-offs at the Arabidopsis WRR4A resistance locus underpin alternate Albugo candida recognition specificities 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.03.29.437434v1?rss=1"
</link>
<description><![CDATA[
The oomycete Albugo candida causes white rust of Brassicaceae, including vegetable and oilseed crops, and wild relatives such as Arabidopsis thaliana. Novel White Rust Resistance (WRR)-genes from Arabidopsis enable new insights into plant/parasite co-evolution. WRR4A from Arabidopsis accession Col-0 provides resistance to many but not all white rust races, and encodes a nucleotide-binding (NB), leucine-rich repeat (LRR) (NLR) immune receptor protein. Col-0 WRR4A resistance is broken by a Col-0-virulent isolate of A. candida race 4 (AcEx1). We identified an allele of WRR4A in Arabidopsis accession Oy-0 and other accessions that confers full resistance to AcEx1. WRR4AOy-0 carries a C-terminal extension required for recognition of AcEx1, but reduces recognition of several effectors recognized by the WRR4ACol-0 allele. WRR4AOy-0 confers full resistance to AcEx1 when expressed as a transgene in the oilseed crop Camelina sativa.

SignificanceA C-terminal extension in an allele of the Arabidopsis resistance-protein WRR4A changes effector recognition specificity, enabling the WRR4AOy-0 allele to confer immunity to Albugo candida races that overcome the WRR4ACol-0 allele. This resistance can be transferred to the oil-producing crop Camelina sativa.

Graphical abstract

O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=137 SRC="FIGDIR/small/437434v1_ufig1.gif" ALT="Figure 1">
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]]></description>
<dc:creator>Castel, B.</dc:creator>
<dc:creator>Fairhead, S.</dc:creator>
<dc:creator>Furzer, O. J.</dc:creator>
<dc:creator>Redkar, A.</dc:creator>
<dc:creator>Wang, S.</dc:creator>
<dc:creator>Cevik, V.</dc:creator>
<dc:creator>Holub, E.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2021-03-29</dc:date>
<dc:identifier>doi:10.1101/2021.03.29.437434</dc:identifier>
<dc:title><![CDATA[Evolutionary trade-offs at the Arabidopsis WRR4A resistance locus underpin alternate Albugo candida recognition specificities]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-03-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.04.14.439785v1?rss=1">
<title>
<![CDATA[
The TCP transcription factor HvTB2 heterodimerizes with VRS5(HvTB1) and controls spike architecture in barley 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.04.14.439785v1?rss=1"
</link>
<description><![CDATA[
Barley is the fourth largest cereal crop grown worldwide, and essential for food and feed production. Phenotypically, the barley spike, which is unbranched, occurs in two main architectural shapes: two-rowed or six-rowed. In the 6-rowed cultivars, all three florets of the triple floret meristem develop into seeds while in 2-rowed lines only the central floret forms a seed. VRS5(HvTB1), act as inhibitor of lateral seed outgrowth and vrs5(hvtb1) mutants display a six-rowed spike architecture. VRS5(HvTB1) is a member of the TCP transcription factor (TF) family, which often form protein-protein interactions with other transcriptional regulators to modulate the expression of their target genes.

Despite the key role of VRS5(HvTB1) in regulating barley plant architecture, there is hardly any knowledge on its molecular mode-of-action. We performed an extensive phylogenetic analysis of the TCP transcription factor family, followed by an in-vitro protein-protein interaction study using yeast-two-hybrid. Our analysis shows that VRS5(HvTB1) has a diverse interaction capacity, interacting with class II TCPs, NF-Y TF, but also chromatin modellers. Further analysis of the interaction capacity of VRS5(HvTB1) with other TCP TFs shows that VRS5(HvTB1) preferably interacts with other class II TCP TFs within the TB1 clade. One of these interactors, encoded by HvTB2, shows a similar expression pattern when compared to VRS5(HvTB1). Haplotype analysis of HvTB2 suggest that this gene is highly conserved and shows hardly any variation in cultivars or wild barley. Induced mutations in HvTB2 trough CRISPR-CAS9 mutagenesis in cv. Golden Promise resulted in barley plants that lost their characteristic unbranched spike architecture. hvtb2 mutants exhibited branches arising at the main spike, suggesting that, similar to VRS5(HvTB1), HvTB2 act as inhibitor of branching. Taken together, our protein-protein interaction studies of VRS5(HvTB1) resulted in the identification of HvTB2, another key regulator of spike architecture in barley. Understanding the molecular network, including protein-protein interactions, of key regulators of plant architecture such as VRS5(HvTB1) provide new routes towards the identification of other key regulators of plant architecture in barley.

Author summaryTranscriptional regulation is one of the basic molecular processes that drives plant growth and development. The key TCP transcriptional regulator TEOSINTE BRANCHED 1 (TB1) is one of these key regulators that has been targeted during domestication of several crops for its role as modulator of branching. Also in barley, a key cereal crop, HvTB1 (also referred to as VRS5), inhibits the outgrowth or side shoots, or tillers, and seeds. Despite its key role in barley development, there is hardly any knowledge on the molecular network that is utilized by VRS5(HvTB1). Transcriptional regulators form homo- and heterodimers to regulate the expression of their downstream targets. Here, we performed an extensive phylogenetic analysis of TCP transcription factors (TFs) in barley, followed by protein-protein interaction studies of VRS5(HvTB1). Our analysis indicates, that VRS5(HvTB1) has a diverse capacity of interacting with class II TCPs, NF-Y TF, but also chromatin modellers. Induced mutagenesis trough CRISPR-CAS mutagenesis of one of the putative VRS5(HvTB1) interactors, HvTB2, resulted in barley plants with branched spikes. This shows that insight into the VRS5(HvTB1) interactome, followed by detailed functional analysis of potential interactors is essential to truly understand how TCPs modulate plant architecture. The study presented here provides a first step to underpin the protein-protein interactome of VRS5(HvTB1) and identify other, yet unknown, key regulators of barley plant architecture.
]]></description>
<dc:creator>de Souza Moraes, T.</dc:creator>
<dc:creator>van Es, S. W.</dc:creator>
<dc:creator>Hernandez-Pinzon, I.</dc:creator>
<dc:creator>Kirschner, G.</dc:creator>
<dc:creator>van der Wal, F.</dc:creator>
<dc:creator>Rodrigues da Silveira, S.</dc:creator>
<dc:creator>Busscher-Lange, J.</dc:creator>
<dc:creator>Angenent, G.</dc:creator>
<dc:creator>Moscou, M.</dc:creator>
<dc:creator>Immink, R.</dc:creator>
<dc:creator>van Esse, W. G.</dc:creator>
<dc:date>2021-04-14</dc:date>
<dc:identifier>doi:10.1101/2021.04.14.439785</dc:identifier>
<dc:title><![CDATA[The TCP transcription factor HvTB2 heterodimerizes with VRS5(HvTB1) and controls spike architecture in barley]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-04-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.05.01.442257v1?rss=1">
<title>
<![CDATA[
ACTIVATION LOOP PHOSPHORYLATION OF A NON-RD RECEPTOR KINASE INITIATES PLANT INNATE IMMUNE SIGNALING 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.05.01.442257v1?rss=1"
</link>
<description><![CDATA[
Receptor kinases (RKs) play fundamental roles in extracellular sensing to regulate development and stress responses across kingdoms. In plants, leucine-rich repeat receptor kinases (LRR-RKs) function primarily as peptide receptors that regulate myriad aspects of plant development and response to external stimuli. Extensive phosphorylation of LRR-RK cytoplasmic domains is among the earliest detectable responses following ligand perception, and reciprocal transphosphorylation between a receptor and its co-receptor is thought to activate the receptor complex. Originally proposed based on characterization of the brassinosteroid receptor, the prevalence of complex activation via reciprocal transphosphorylation across the plant RK family has not been tested. Using the LRR-RK ELONGATION FACTOR TU RECEPTOR (EFR) as a model RK, we set out to understand the steps critical for activating RK complexes. While the EFR cytoplasmic domain is an active protein kinase in vitro and is phosphorylated in a ligand-dependent manner in vivo, catalytically deficient EFR variants are functional in anti-bacterial immunity. These results reveal a non-catalytic role for the EFR cytoplasmic domain in triggering immune signaling and indicate that reciprocal transphoshorylation is not a ubiquitous requirement for LRR-RK complex activation. Rather, our analysis of EFR along with a detailed survey of the literature suggests a distinction between LRR-RK complexes with RD- versus non-RD protein kinase domains. Based on newly identified phosphorylation sites that regulate the activation state of the EFR complex in vivo, we propose that LRR-RK complexes containing a non-RD protein kinase may be regulated by phosphorylation-dependent conformational changes of the ligand-binding receptor which could initiate signaling in a feed-forward fashion either allosterically or through driving the dissociation of negative regulators of the complex.
]]></description>
<dc:creator>Bender, K. W.</dc:creator>
<dc:creator>Couto, D.</dc:creator>
<dc:creator>Kadota, Y.</dc:creator>
<dc:creator>Macho, A. P.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Bjornson, M.</dc:creator>
<dc:creator>Petriello, A.</dc:creator>
<dc:creator>Font Farre, M.</dc:creator>
<dc:creator>Schwessinger, B.</dc:creator>
<dc:creator>Ntoukakis, V.</dc:creator>
<dc:creator>Stransfeld, L.</dc:creator>
<dc:creator>Jones, A. M. E.</dc:creator>
<dc:creator>Menke, F. L.</dc:creator>
<dc:creator>zipfel, c.</dc:creator>
<dc:date>2021-05-01</dc:date>
<dc:identifier>doi:10.1101/2021.05.01.442257</dc:identifier>
<dc:title><![CDATA[ACTIVATION LOOP PHOSPHORYLATION OF A NON-RD RECEPTOR KINASE INITIATES PLANT INNATE IMMUNE SIGNALING]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-05-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.05.20.444601v1?rss=1">
<title>
<![CDATA[
The immune Rysto receptor recognizes a broadly conserved feature of potyviral coat proteins 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.05.20.444601v1?rss=1"
</link>
<description><![CDATA[
Potyviruses are the largest group of plant RNA viruses, causing significant losses in many crops. Among them, potato virus Y (PVY) is particularly important, and enhances the severity of infections by other viruses. The Rysto gene confers PVY resistance and encodes a TIR-NLR intracellular immune receptors that recognizes PVY coat protein (CP). To define a minimal CP fragment sensed by Rysto, we created a series of truncated CP variants and expressed these CP derivatives in Rysto transgenic plants. Deletions that affect the 149 amino acid CP core region lose the ability to trigger Rysto-dependent defence activation. Furthermore, point mutations in the amino acid residues Ser126, Arg157, and Asp201 of the highly conserved RNA-binding pocket of potyviral CP, reduce or abolish Rysto-dependent responses, demonstrating that appropriate folding of the CP core is required for Rysto-mediated recognition. Consistent with these data, we found Rysto recognises CPs of various viruses that share a similar core region, but not those lacking it. Finally, we demonstrated that Rysto provides immunity to plum pox virus and turnip mosaic virus, demonstrating its wide range of applications in disease-resistant crop engineering. In parallel, we showed that CP triggered Rysto activation is SAG101- but not PAD4- or SA-level dependent. Our findings shed new light on how R proteins can detect viruses by sensing highly conserved structural patterns.
]]></description>
<dc:creator>Grech-Baran, M.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Poznanski, J.</dc:creator>
<dc:creator>Grupa-Urbanska, A.</dc:creator>
<dc:creator>Malinowski, T.</dc:creator>
<dc:creator>Lichocka, M.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Hennig, J.</dc:creator>
<dc:date>2021-05-21</dc:date>
<dc:identifier>doi:10.1101/2021.05.20.444601</dc:identifier>
<dc:title><![CDATA[The immune Rysto receptor recognizes a broadly conserved feature of potyviral coat proteins]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-05-21</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.06.10.447899v1?rss=1">
<title>
<![CDATA[
Rpi-amr3 confers resistance to multiple Phytophthora species by recognizing a conserved RXLR effector 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.06.10.447899v1?rss=1"
</link>
<description><![CDATA[
Diverse pathogens from the genus Phytophthora cause disease and reduce yields in many crop plants. Although many Resistance to Phytophthora infestans (Rpi) genes effective against potato late blight have been cloned, few have been cloned against other Phytophthora species. Most Rpi genes encode nucleotide-binding domain, leucine-rich repeat-containing (NLR) proteins, that recognize RXLR effectors. However, whether NLR proteins can recognize RXLR effectors from multiple different Phytophthora pathogens has rarely been investigated. Here, we report the effector AVRamr3 from P. infestans that is recognized by Rpi-amr3 from S. americanum. We show here that AVRamr3 is broadly conserved in many different Phytophthora species, and that recognition of AVRamr3 homologs enables resistance against multiple Phytophthora pathogens, including P. parasitica and P. palmivora. Our findings suggest a novel path to identifying R genes against important plant pathogens.
]]></description>
<dc:creator>Lin, X.</dc:creator>
<dc:creator>Olave-Achury, A.</dc:creator>
<dc:creator>Heal, R.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Karki, H. S.</dc:creator>
<dc:creator>Song, T.</dc:creator>
<dc:creator>Wu, C.-h.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Vleeshouwers, V. G. A. A.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2021-06-10</dc:date>
<dc:identifier>doi:10.1101/2021.06.10.447899</dc:identifier>
<dc:title><![CDATA[Rpi-amr3 confers resistance to multiple Phytophthora species by recognizing a conserved RXLR effector]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-06-10</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.06.18.449010v1?rss=1">
<title>
<![CDATA[
Pseudomonas syringae addresses distinct environmental challenges during plant infection through the coordinated deployment of polysaccharides 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.06.18.449010v1?rss=1"
</link>
<description><![CDATA[
Prior to infection, phytopathogenic bacteria face a challenging environment on the plant surface, where they are exposed to nutrient starvation and abiotic stresses. Pathways enabling surface adhesion, stress tolerance and epiphytic survival are important for successful plant pathogenesis. Understanding the roles and regulation of these pathways is therefore crucial to fully understand bacterial plant infections. The phytopathogen Pseudomonas syringae pv. tomato (Pst) encodes multiple polysaccharides that are implicated in biofilm formation, stress survival and virulence in other microbes. To examine how these polysaccharides impact Pst epiphytic survival and pathogenesis, we analysed mutants in multiple polysaccharide loci to determine their intersecting contributions to epiphytic survival and infection. In parallel, we used qRT-PCR to analyse the regulation of each pathway. Pst polysaccharides are tightly coordinated by multiple environmental signals. Nutrient availability, temperature and surface association strongly affect the expression of different polysaccharides under the control of the signalling proteins ladS and cbrB and the second messenger cyclic-di-GMP. Furthermore, functionally redundant, combinatorial phenotypes were observed for several polysaccharides. Exopolysaccharides and WapQ-mediated lipopolysaccharide production are important for leaf adhesion, while -glucan and alginate together confer desiccation tolerance. Our results suggest that polysaccharides play important roles in overcoming environmental challenges to Pst during plant infection.

HighlightPseudomonas syringae uses the coordinated deployment of polysaccharides to address environmental challenges during plant colonization. Functional redundancy renders individual polysaccharides dispensable during plant infection, but their combined loss impedes pathogenicity.
]]></description>
<dc:creator>Pilla, S. K.</dc:creator>
<dc:creator>Woodcock, S. D.</dc:creator>
<dc:creator>Pfeilmeier, S.</dc:creator>
<dc:creator>Borneman, S.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Malone, J. G.</dc:creator>
<dc:date>2021-06-18</dc:date>
<dc:identifier>doi:10.1101/2021.06.18.449010</dc:identifier>
<dc:title><![CDATA[Pseudomonas syringae addresses distinct environmental challenges during plant infection through the coordinated deployment of polysaccharides]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-06-18</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.06.25.449940v1?rss=1">
<title>
<![CDATA[
Functional diversification gave rise to allelic specialization in a rice NLR immune receptor pair 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.06.25.449940v1?rss=1"
</link>
<description><![CDATA[
Cooperation between receptors from the NLR superfamily is important for intracellular activation of immune responses. NLRs can function in pairs that, upon pathogen recognition, trigger hypersensitive cell death and stop pathogen invasion. Natural selection drives specialization of host immune receptors towards an optimal response, whilst keeping a tight regulation of immunity in the absence of pathogens. However, the molecular basis of co-adaptation and specialization between paired NLRs remains largely unknown. Here, we describe functional specialization in alleles of the rice NLR pair Pik that confers resistance to strains of the blast fungus Magnaporthe oryzae harbouring AVR-Pik effectors. We revealed that matching pairs of allelic Pik NLRs mount effective immune responses whereas mismatched pairs lead to autoimmune phenotypes, a hallmark of hybrid necrosis in both natural and domesticated plant populations. We further showed that allelic specialization is largely underpinned by a single amino acid polymorphism that determines preferential association between matching pairs of Pik NLRs. These results provide a framework for how functionally linked immune receptors undergo co-adaptation to provide an effective and regulated immune response against pathogens. Understanding the molecular constraints that shape paired NLR evolution has implications beyond plant immunity given that hybrid necrosis can drive reproductive isolation.
]]></description>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Benjumea, J. V.</dc:creator>
<dc:creator>Bialas, A.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2021-06-25</dc:date>
<dc:identifier>doi:10.1101/2021.06.25.449940</dc:identifier>
<dc:title><![CDATA[Functional diversification gave rise to allelic specialization in a rice NLR immune receptor pair]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-06-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.07.28.454147v1?rss=1">
<title>
<![CDATA[
Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor. 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.07.28.454147v1?rss=1"
</link>
<description><![CDATA[
Plants use intracellular immune receptors (NLRs) to detect pathogen-derived effector proteins. The Arabidopsis NLR pair RRS1-R/RPS4 confers disease resistance to different bacterial pathogens by perceiving structurally distinct effectors AvrRps4 from Pseudomonas syringae pv. pisi and PopP2 from Ralstonia solanacearum via an integrated WRKY domain in RRS1-R. How the WRKY domain of RRS1 (RRS1WRKY) perceives distinct classes of effector to initiate an immune response is unknown. We report here the crystal structure of the in planta processed C-terminal domain of AvrRps4 (AvrRps4C) in complex with RRS1WRKY. Perception of AvrRps4C by RRS1WRKY is mediated by the {beta}2-{beta}3 segment of RRS1WRKY that binds an electronegative patch on the surface of AvrRps4C. Structure-based mutations that disrupt AvrRps4C/RRS1WRKY interactions in vitro compromise RRS1/RPS4-dependent immune responses. We also show that AvrRps4C can associate with the WRKY domain of the related but distinct RRS1B/RPS4B NLR pair, and the DNA binding domain of AtWRKY41, with similar binding affinities. This work demonstrates how integrated domains in plant NLRs can directly bind structurally distinct effectors to initiate immunity.

SignificanceThis study reveals a mechanism of effector recognition by a plant NLR immune receptor that carries an integrated domain (ID) which mimics an authentic pathogen effector target. An Arabidopsis immune receptor carrying RRS1 and RPS4 NLR proteins detects the Pseudomonas syringae pv. pisi secreted effector AvrRps4 via a WRKY ID in RRS1. We used structural biology to reveal the mechanisms of AvrRps4/WRKY interaction and demonstrated that this binding is essential for effector recognition in planta. Our analysis revealed distinctive features of the WRKY ID that mediate the recognition of structurally distinct effectors from different bacterial pathogens. These insights could enable engineering NLRs with novel recognition specificities, and enhances our understanding of how effectors interact with host proteins.
]]></description>
<dc:creator>Mukhi, N.</dc:creator>
<dc:creator>Brown, H.</dc:creator>
<dc:creator>Gorenkin, D.</dc:creator>
<dc:creator>Ding, P.</dc:creator>
<dc:creator>Bentham, A. R.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2021-07-28</dc:date>
<dc:identifier>doi:10.1101/2021.07.28.454147</dc:identifier>
<dc:title><![CDATA[Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor.]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-07-28</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.08.10.455798v1?rss=1">
<title>
<![CDATA[
pOPIN-GG: A resource for modular assembly in protein expression vectors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.08.10.455798v1?rss=1"
</link>
<description><![CDATA[
The ability to recombinantly produce target proteins is essential to many biochemical, structural, and biophysical assays that allow for interrogation of molecular mechanisms behind protein function. Purification and solubility tags are routinely used to maximise the yield and ease of protein expression and purification from E. coli. A major hurdle in high-throughput protein expression trials is the cloning required to produce multiple constructs with different solubility tags. Here we report a modification of the well-established pOPIN expression vector suite to be compatible with modular cloning via Type IIS restriction enzymes. This allows users to rapidly generate multiple constructs with any desired tag, introducing modularity in the system and delivering compatibility with other modular cloning vector systems, for example streamlining the process of moving between expression hosts. We demonstrate these constructs maintain the expression capability of the original pOPIN vector suite and can also be used to efficiently express and purify protein complexes, making these vectors an excellent resource for high-throughput protein expression trials.

HighlightsO_LIpOPIN-GG expression vectors allow for modular cloning enabling rapid screening of purification and solubility tags at no loss of expression compared to previous vectors.
C_LIO_LICloning into the pOPIN-GG vectors can be performed from PCR products or from level 0 vectors containing the required parts.
C_LIO_LISeveral vectors with different resistances and origins of replication have been generated allowing the effective co-expression and purification of protein complexes.
C_LIO_LIAll pOPIN-GG vectors generated here are available on Addgene, as well as level 0 acceptors and tags.
C_LI
]]></description>
<dc:creator>Bentham, A. R.</dc:creator>
<dc:creator>Youles, M.</dc:creator>
<dc:creator>Mendel, M. N.</dc:creator>
<dc:creator>Varden, F. A.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2021-08-10</dc:date>
<dc:identifier>doi:10.1101/2021.08.10.455798</dc:identifier>
<dc:title><![CDATA[pOPIN-GG: A resource for modular assembly in protein expression vectors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-08-10</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.08.29.457830v1?rss=1">
<title>
<![CDATA[
Conserved secreted effectors determine endophytic growth and multi-host plant compatibility in a vascular wilt fungus 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.08.29.457830v1?rss=1"
</link>
<description><![CDATA[
Fungal interactions with plant roots, either beneficial or detrimental, have a major impact on agriculture and ecosystems. The soil inhabiting ascomycete Fusarium oxysporum (Fo) constitutes a species complex of worldwide distribution causing vascular wilt in more than a hundred different crops. Individual isolates of the fungus exhibit host-specific pathogenicity, determined by proteinaceous effectors termed secreted in xylem (SIX). However, such isolates can also colonize roots of non-host plants asymptomatically as endophytes, or even protect them against pathogenic isolates. The molecular determinants of multi-host plant colonization are currently unknown. Here, we identified a set of fungal effectors termed ERCs (Early Root Compatibility effectors), which are secreted during early biotrophic growth of Fo on both host and non-host plants. In contrast to the strain-specific SIX effectors, which are encoded on accessory genomic regions, ERCs are encoded on core regions and are found across the entire Fo species complex as well as in other phytopathogens, suggesting a conserved role in fungus-plant associations. Targeted deletion of ERC genes in a pathogenic Fo isolate resulted in reduced virulence on the host plant and rapid activation of plant immune responses, while in a non-pathogenic isolate it led to impaired root colonization and loss of biocontrol ability. Strikingly, some ERCs also contribute to Fo infection on the non-vascular land plant Marchantia polymorpha. Our results reveal an evolutionarily conserved mechanism for multi-host colonization by root infecting fungi.
]]></description>
<dc:creator>Redkar, A.</dc:creator>
<dc:creator>Sabale, M.</dc:creator>
<dc:creator>Schudoma, C.</dc:creator>
<dc:creator>Zechmann, B.</dc:creator>
<dc:creator>Gupta, Y. K.</dc:creator>
<dc:creator>Lopez-Berges, M. S.</dc:creator>
<dc:creator>Venturini, G.</dc:creator>
<dc:creator>Gimenez Ibanez, S.</dc:creator>
<dc:creator>Turra, D.</dc:creator>
<dc:creator>Solano, R.</dc:creator>
<dc:creator>Di Pietro, A.</dc:creator>
<dc:date>2021-08-29</dc:date>
<dc:identifier>doi:10.1101/2021.08.29.457830</dc:identifier>
<dc:title><![CDATA[Conserved secreted effectors determine endophytic growth and multi-host plant compatibility in a vascular wilt fungus]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-08-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.08.11.455944v1?rss=1">
<title>
<![CDATA[
A CCaMK/Cyclops response element in the promoter of L. japonicus Calcium-Binding Protein 1 (CBP1) mediates transcriptional activation in root symbioses 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.08.11.455944v1?rss=1"
</link>
<description><![CDATA[
Early gene expression in arbuscular mycorrhiza (AM) and the nitrogen-fixing root nodule symbiosis (RNS) is governed by a shared regulatory complex. Yet many symbiosis-induced genes are specifically activated in only one of the two symbioses. The Lotus japonicus T-DNA insertion line T90, carrying a promoterless uidA (GUS) gene in the promoter of Calcium Binding Protein1 (CBP1) is exceptional as it exhibits GUS activity in both root endosymbioses. To identify the responsible cis- and trans-acting factors, we subjected deletion/modification series of CBP1 promoter:reporter fusions to transactivation and spatio-temporal expression analysis and screened EMS-mutagenized T90 populations for aberrant GUS expression. We identified one cis-regulatory element required for GUS expression in the epidermis and a second element, necessary and sufficient for transactivation by the Calcium and Calmodulin-dependent protein kinase (CCaMK) in combination with the transcription factor Cyclops and conferring gene expression during both AM and RNS. Lack of GUS expression in T90 white mutants could be traced to DNA hypermethylation detected in and around this element. We concluded that the CCaMK/Cyclops complex can contribute to at least three distinct gene expression patterns on its direct target promoters NIN (RNS), RAM1 (AM), and CBP1 (AM and RNS), calling for yet-to-be identified specificity-conferring factors.
]]></description>
<dc:creator>Gong, X.</dc:creator>
<dc:creator>Bucerius, S.</dc:creator>
<dc:creator>Jensen, E.</dc:creator>
<dc:creator>Parniske, M.</dc:creator>
<dc:date>2021-08-11</dc:date>
<dc:identifier>doi:10.1101/2021.08.11.455944</dc:identifier>
<dc:title><![CDATA[A CCaMK/Cyclops response element in the promoter of L. japonicus Calcium-Binding Protein 1 (CBP1) mediates transcriptional activation in root symbioses]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-08-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.08.30.457756v1?rss=1">
<title>
<![CDATA[
S-acylation is a positive regulator of FLS2-mediated plant immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.08.30.457756v1?rss=1"
</link>
<description><![CDATA[
Plant receptor kinases are key transducers of extracellular stimuli, such as the presence of beneficial or pathogenic microbes or secreted signalling molecules. Receptor kinases are regulated by numerous post-translational modifications. Here, using the immune receptor kinases FLS2 and EFR, we show that S-acylation at a cysteine conserved in all plant receptor kinases is crucial for function. S-acylation involves the addition of long-chain fatty acids to cysteine residues within proteins, altering their biophysical properties and behaviour within the membrane environment. We observe S-acylation of FLS2 at C-terminal kinase domain cysteine residues within minutes following perception of its ligand flg22, in a BAK1 co-receptor dependent manner. We demonstrate that S-acylation is essential for FLS2-mediated immune signalling and resistance to bacterial infection. Similarly, mutating the corresponding conserved cysteine residue in EFR supressed elf18 triggered signalling. Analysis of unstimulated and activated FLS2-containing complexes using microscopy, detergents and native membrane DIBMA nanodiscs indicates that S-acylation stabilises and promotes retention of activated receptor kinase complexes at the plasma membrane to increase signalling efficiency.
]]></description>
<dc:creator>Hurst, C. H.</dc:creator>
<dc:creator>Turnbull, D.</dc:creator>
<dc:creator>Gronnier, J.</dc:creator>
<dc:creator>Myles, S.</dc:creator>
<dc:creator>Pflughaupt, R. L.</dc:creator>
<dc:creator>Kopischke, M.</dc:creator>
<dc:creator>Davies, P.</dc:creator>
<dc:creator>Jones, S.</dc:creator>
<dc:creator>Robatzek, S.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Hemsley, P.</dc:creator>
<dc:date>2021-08-31</dc:date>
<dc:identifier>doi:10.1101/2021.08.30.457756</dc:identifier>
<dc:title><![CDATA[S-acylation is a positive regulator of FLS2-mediated plant immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-08-31</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.09.01.458560v1?rss=1">
<title>
<![CDATA[
A genetically linked pair of NLR immune receptors show contrasting patterns of evolution 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.09.01.458560v1?rss=1"
</link>
<description><![CDATA[
Throughout their evolution, plant nucleotide-binding leucine-rich-repeat receptors (NLRs) have acquired widely divergent unconventional integrated domains that enhance their ability to detect pathogen effectors. However, the functional dynamics that drive the evolution of NLRs with integrated domains (NLR-IDs) remain poorly understood. Here, we reconstructed the evolutionary history of an NLR locus prone to unconventional domain integration and experimentally tested hypotheses about the evolution of NLR-IDs. We show that the rice (Oryza sativa) NLR Pias recognizes the effector AVR-Pias of the blast fungal pathogen Magnaporthe oryzae. Pias consists of a functionally specialized NLR pair, the helper Pias-1 and the sensor Pias-2, that is allelic to the previously characterized Pia pair of NLRs: the helper RGA4 and the sensor RGA5. Remarkably, Pias-2 carries a C-terminal DUF761 domain at a similar position to the heavy metal-associated (HMA) domain of RGA5. Phylogenomic analysis showed that Pias-2/RGA5 sensor NLRs have undergone recurrent genomic recombination within the genus Oryza, resulting in up to six sequence-divergent domain integrations. Allelic NLRs with divergent functions have been maintained trans-species in different Oryza lineages to detect sequence-divergent pathogen effectors. By contrast, Pias-1 has retained its NLR helper activity throughout evolution and is capable of functioning together with the divergent sensor-NLR RGA5 to responds to AVR-Pia. These results suggest that opposite selective forces have driven the evolution of paired NLRs: highly dynamic domain integration events maintained by balancing selection for sensor NLRs, in sharp contrast to purifying selection and functional conservation of immune signaling for helper NLRs.

Significance statementPlants have evolved sophisticated defense mechanisms to fend off pathogens. Plant nucleotide-binding leucine-rich repeat receptor (NLR) proteins play crucial roles in detecting pathogen molecules inside plant cells and mounting defense responses. Here, we identified the Pias gene from rice, which encodes the NLR pair Pias-1 "helper" and Pias-2 "sensor." These proteins function together to detect the pathogen molecule AVR-Pias of Magnaporthe oryzae and defend against rice blast disease. Pias is allelic to the previously reported Pia gene. A comparison of Pias/Pia alleles among Oryza species showed that Pias/Pia helper is evolutionarily and functionally conserved, whereas the Pias/Pia sensor shows highly dynamic evolution, with various host domains integrated into similar positions, allowing it to detect a wide variety of pathogen molecules.
]]></description>
<dc:creator>Shimizu, M.</dc:creator>
<dc:creator>Hirabuchi, A.</dc:creator>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:creator>Abe, A.</dc:creator>
<dc:creator>Takeda, T.</dc:creator>
<dc:creator>Kobayashi, M.</dc:creator>
<dc:creator>Hiraka, Y.</dc:creator>
<dc:creator>Kanzaki, E.</dc:creator>
<dc:creator>Oikawa, K.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:date>2021-09-02</dc:date>
<dc:identifier>doi:10.1101/2021.09.01.458560</dc:identifier>
<dc:title><![CDATA[A genetically linked pair of NLR immune receptors show contrasting patterns of evolution]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-09-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.09.28.461843v1?rss=1">
<title>
<![CDATA[
The helper NLR immune protein NRC3 mediates the hypersensitive cell death caused by the cell-surface receptor Cf-4 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.09.28.461843v1?rss=1"
</link>
<description><![CDATA[
Cell surface pattern recognition receptors (PRRs) activate immune responses that can include the hypersensitive cell death. However, the pathways that link PRRs to the cell death response are poorly understood. Here, we show that the cell surface receptor-like protein Cf-4 requires the intracellular nucleotide-binding domain leucine-rich repeat containing receptor (NLR) NRC3 to trigger a confluent cell death response upon detection of the fungal effector Avr4 in leaves of Nicotiana benthamiana. This NRC3 activity requires an intact N-terminal MADA motif, a conserved signature of coiled-coil (CC)-type plant NLRs that is required for resistosome-mediated immune responses. A chimeric protein with the N-terminal 1 helix of Arabidopsis ZAR1 swapped into NRC3 retains the capacity to mediate Cf-4 hypersensitive cell death. Pathogen effectors acting as suppressors of NRC3 can suppress Cf-4-triggered hypersensitive cell-death. Our findings link the NLR resistosome model to the hypersensitive cell death caused by a cell surface PRR.
]]></description>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2021-09-28</dc:date>
<dc:identifier>doi:10.1101/2021.09.28.461843</dc:identifier>
<dc:title><![CDATA[The helper NLR immune protein NRC3 mediates the hypersensitive cell death caused by the cell-surface receptor Cf-4]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-09-28</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.09.06.459143v1?rss=1">
<title>
<![CDATA[
Novel effector recognition capacity engineered into a paired NLR complex 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.09.06.459143v1?rss=1"
</link>
<description><![CDATA[
The Arabidopsis RRS1-R Resistance gene confers recognition of the bacterial acetyltransferase PopP2 and another bacterial effector, AvrRps4. The RRS1-S allele recognizes AvrRps4 but not PopP2. RRS1- R/RRS1-S heterozygotes cannot recognize PopP2. RRS1-R and RRS1-S also suppress the constitutive RPS4-dependent autoactivity of RRS1-Rslh1. Phytoplasmas cause important plant diseases, and their effectors can cause degradation of specific host proteins. We tested whether attaching a pathogen effector-dependent degron to RRS1-R, enabling its degradation by phytoplasma effector SAP05, could derepress RRS1-Rslh1 autoactivity, resulting in SAP05-dependent resistance. In transient assays in tobacco, RRS1-R-derived constructs can confer a hypersensitive response (HR) to SAP05. However, phytoplasma infection assays in transgenic Arabidopsis resulted in delayed disease symptoms but not full resistance. We provide a proof-of-concept strategy utilizing the recessiveness of a plant immune receptor gene to engineer recognition of a pathogen effector that promotes degradation of a specific host protein.
]]></description>
<dc:creator>Wang, S.</dc:creator>
<dc:creator>Huang, W.</dc:creator>
<dc:creator>Duxbury, Z.</dc:creator>
<dc:creator>Hogenhout, S. A.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2021-09-06</dc:date>
<dc:identifier>doi:10.1101/2021.09.06.459143</dc:identifier>
<dc:title><![CDATA[Novel effector recognition capacity engineered into a paired NLR complex]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-09-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.09.29.461190v1?rss=1">
<title>
<![CDATA[
A NET4-RabG3 couple mediate the link between actin and the tonoplast and is essential for normal actin cytoskeletal remodelling in stomatal closure to flg22 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.09.29.461190v1?rss=1"
</link>
<description><![CDATA[
Members of the NETWORKED (NET) family are involved in actin-membrane interactions. They tether the cells plasma membrane (PM) to the actin network. Moreover, in a similar manner, they are also involved in the tethering of membrane bound organelles to the actin cytoskeleton; the endoplasmic reticulum (ER) and the ER to the PM. This raises the question as to whether NET proteins are involved in actin cytoskeletal remodelling. Here we show that two members of the NET family, NET4A and NET4B, are essential for normal guard cell actin reorganization, which is a process critical for stomatal closure in plant immunity. NET4 proteins interact with F-actin and with members of the Rab7 GTPase RABG3 family through two distinct domains, allowing for simultaneous localization to actin filaments and the tonoplast. NET4 proteins interact with GTP-bound, active RABG3 members, suggesting their function as downstream effectors. We also show that RABG3b is critical for stomatal closure induced by microbial patterns. Taken together, we conclude that the actin cytoskeletal remodelling during stomatal closure depends on a molecular link between actin filaments and the tonoplast, which is mediated by the NET4-RABG3b interaction. We propose that stomatal closure to microbial patterns involves the coordinated action of immune signalling events and proper actin cytoskeletal remodelling.
]]></description>
<dc:creator>HAWKINS, T. J.</dc:creator>
<dc:creator>Kopischke, M.</dc:creator>
<dc:creator>Mentlak, D.</dc:creator>
<dc:creator>Duckney, P.</dc:creator>
<dc:creator>Kroon, J.</dc:creator>
<dc:creator>Bui, M. T.</dc:creator>
<dc:creator>Richardson, C.</dc:creator>
<dc:creator>Casey, M.</dc:creator>
<dc:creator>Alexander, A.</dc:creator>
<dc:creator>De Jaeger, G.</dc:creator>
<dc:creator>Kalde, M.</dc:creator>
<dc:creator>Moore, I.</dc:creator>
<dc:creator>Dagdas, Y.</dc:creator>
<dc:creator>Hussey, P. J.</dc:creator>
<dc:creator>Robatzek, S.</dc:creator>
<dc:date>2021-09-30</dc:date>
<dc:identifier>doi:10.1101/2021.09.29.461190</dc:identifier>
<dc:title><![CDATA[A NET4-RabG3 couple mediate the link between actin and the tonoplast and is essential for normal actin cytoskeletal remodelling in stomatal closure to flg22]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-09-30</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.10.04.463104v1?rss=1">
<title>
<![CDATA[
Regressive evolution of an effector following a host jump in the Irish Potato Famine Pathogen Lineage 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.10.04.463104v1?rss=1"
</link>
<description><![CDATA[
In order to infect a new host species, the pathogen must evolve to enhance infection and transmission in the novel environment. Although we often think of evolution as a process of accumulation, it is also a process of loss. Here, we document an example of regressive evolution in the Irish potato famine pathogen (Phytophthora infestans) lineage, providing evidence that a key sequence motif in the effector PexRD54 has degenerated following a host jump. We began by looking at PexRD54 and PexRD54-like sequences from across Phytophthora species. We found that PexRD54 emerged in the common ancestor of Phytophthora clade 1b and 1c species, and further sequence analysis showed that a key functional motif, the C-terminal ATG8-interacting motif (AIM), was also acquired at this point in the lineage. A closer analysis showed that the P. mirabilis PexRD54 (PmPexRD54) AIM appeared unusual, the otherwise-conserved central residue mutated from a glutamate to a lysine. We aimed to determine whether this PmPexRD54 AIM polymorphism represented an adaptation to the Mirabilis jalapa host environment. We began by characterizing the M. jalapa ATG8 family, finding that they have a unique evolutionary history compared to previously characterized ATG8s. Then, using co-immunoprecipitation and isothermal titration calorimetry assays, we showed that both full-length PmPexRD54 and the PmPexRD54 AIM peptide bind very weakly to the M. jalapa ATG8s. Through a combination of binding assays and structural modelling, we showed that the identity of the residue at the position of the PmPexRD54 AIM polymorphism can underpin high-affinity binding to plant ATG8s. Finally, we conclude that the functionality of the PexRD54 AIM was lost in the P. mirabilis lineage, perhaps owing to as-yet-unknown pressure on this effector in the new host environment.

Author SummaryPathogens evolve in concert with their hosts. When a pathogen begins to infect a new host species, known as a "host jump," the pathogen must evolve to enhance infection and transmission. These evolutionary processes can involve both the gain and loss of genes, as well as dynamic changes in protein function. Here, we describe an example of a pathogen protein that lost a key functional domain following a host jump, a salient example of "regressive evolution." Specifically, we show that an effector protein from the plant pathogen Phytopthora mirabilis, a host-specific lineage closely related to the Irish potato famine pathogen Phytopthora infestans, has a derived amino acid polymorphism that results in a loss of interaction with certain host machinery.
]]></description>
<dc:creator>Zess, E. K.</dc:creator>
<dc:creator>Dagdas, Y. F.</dc:creator>
<dc:creator>Peers, E.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2021-10-05</dc:date>
<dc:identifier>doi:10.1101/2021.10.04.463104</dc:identifier>
<dc:title><![CDATA[Regressive evolution of an effector following a host jump in the Irish Potato Famine Pathogen Lineage]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-10-05</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.10.08.463641v1?rss=1">
<title>
<![CDATA[
Chloroplast movement and positioning protein CHUP1 is required for focal immunity against Phytophthora infestans 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.10.08.463641v1?rss=1"
</link>
<description><![CDATA[
Communication between cellular organelles is essential for mounting effective innate immune responses to eliminate pathogens. In plants, the transport of cellular organelles to pathogen penetration sites and their assembly around the host membrane delineating plant-pathogen interface are well-documented. However, whether organelles associate with these specialized plant-pathogen membrane interfaces and the extent to which this process contributes to immunity remain unknown. Here, we discovered defense-related membrane contact sites (MCS) comprising a membrane tethering complex between chloroplasts and the extrahaustorial membrane (EHM) surrounding the pathogen haustorium. The assembly of this membrane tethering complex relies on the association between the chloroplast outer envelope protein CHLOROPLAST UNUSUAL POSITIONING 1 (CHUP1), and its plasma membrane-associated partner, KINESIN-LIKE PROTEIN FOR ACTIN-BASED CHLOROPLAST MOVEMENT 1 (KAC1). Our biochemical assays revealed that CHUP1 and KAC1 interact, while infection cell biology demonstrated their co-accumulation in foci where chloroplasts contact the EHM. Genetic depletion of CHUP1 or KAC1 reduces the deposition of callose--a cell wall material typically deployed to fortify pathogen penetration resistance--around the haustorium, without affecting other core immune processes. Our findings suggest that the chloroplast-EHM attachment complex positively regulates plant focal immunity, revealing the key components and their potential roles in the targeted deposition of defense components at the pathogen interface. These results advance our understanding of organelle-mediated immune responses and highlight the significance of MCS in plant-pathogen interactions.
]]></description>
<dc:creator>Savage, Z.</dc:creator>
<dc:creator>Erickson, J. L.</dc:creator>
<dc:creator>Prautsch, J.</dc:creator>
<dc:creator>Balmez, A. I.</dc:creator>
<dc:creator>Tumtas, Y.</dc:creator>
<dc:creator>Yuen, E. L. H.</dc:creator>
<dc:creator>Stuttmann, J.</dc:creator>
<dc:creator>Fantino, E.</dc:creator>
<dc:creator>Duggan, C.</dc:creator>
<dc:creator>Molinari, C.</dc:creator>
<dc:creator>Schattat, M.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:date>2021-10-09</dc:date>
<dc:identifier>doi:10.1101/2021.10.08.463641</dc:identifier>
<dc:title><![CDATA[Chloroplast movement and positioning protein CHUP1 is required for focal immunity against Phytophthora infestans]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-10-09</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.10.24.465418v1?rss=1">
<title>
<![CDATA[
NLR immune receptor-nanobody fusions confer plant disease resistance 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.10.24.465418v1?rss=1"
</link>
<description><![CDATA[
Plant pathogens cause recurrent epidemics that threaten crop yield and global food security. Efforts to retool the plant immune system have been limited to modifying natural components and can be nullified by the emergence of new pathogen races. Therefore, there is a need to develop made-to-order synthetic plant immune receptors with resistance tailored to the pathogen genotypes present in the field. Here we show that plant immune receptors can be used as scaffolds for VHH nanobody fusions that bind fluorescent proteins (FPs). The receptor-nanobody fusions signal in the presence of the corresponding FP and confer resistance against plant viruses expressing FPs. Given that nanobodies can be raised against virtually any molecule, immune receptor-nanobody fusions have the potential to generate resistance against all major plant pathogens and pests.

One-Sentence SummaryPlant immune receptor-nanobody fusions enable made-to-order disease resistance genes.
]]></description>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Marchal, C.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2021-10-24</dc:date>
<dc:identifier>doi:10.1101/2021.10.24.465418</dc:identifier>
<dc:title><![CDATA[NLR immune receptor-nanobody fusions confer plant disease resistance]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-10-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.10.25.465685v1?rss=1">
<title>
<![CDATA[
Perception of a conserved family of plant signalling peptides by the receptor kinase HSL3 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.10.25.465685v1?rss=1"
</link>
<description><![CDATA[
Plant genomes encode hundreds of secreted peptides; however, relatively few have been characterised. We report here an uncharacterised, stress-induced family of plant signalling peptides, which we call CTNIPs. Based on the role of the common co-receptor BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1) in CTNIP-induced responses, we identified the orphan receptor kinase HAESA-LIKE 3 (HSL3) as the CTNIP receptor via a proteomics approach. CTNIP binding, ligand-triggered complex formation with BAK1, and induced downstream responses all involve HSL3. Notably, the HSL3-CTNIP signalling module is evolutionarily ancient, predating the divergence of extant angiosperms. The identification of this signalling module will help establish its physiological role and provides a resource to understand further receptor-ligand co-evolution.
]]></description>
<dc:creator>Rhodes, J.</dc:creator>
<dc:creator>Roman, A.-O.</dc:creator>
<dc:creator>Bjornson, M.</dc:creator>
<dc:creator>Brandt, B.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Wyler, M.</dc:creator>
<dc:creator>Schmid, M.</dc:creator>
<dc:creator>Menke, F. L.</dc:creator>
<dc:creator>Santiago, J.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2021-10-26</dc:date>
<dc:identifier>doi:10.1101/2021.10.25.465685</dc:identifier>
<dc:title><![CDATA[Perception of a conserved family of plant signalling peptides by the receptor kinase HSL3]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-10-26</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.11.15.468391v1?rss=1">
<title>
<![CDATA[
An atypical NLR protein modulates the NRC immune receptor network 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.11.15.468391v1?rss=1"
</link>
<description><![CDATA[
The NRC immune receptor network has evolved in asterid plants from a pair of linked genes into a genetically dispersed and phylogenetically structured network of sensor and helper NLR (nucleotide-binding domain and leucine-rich repeat-containing) proteins. In some species, such as the model plant Nicotiana benthamiana and other Solanaceae, the NRC network forms up to half of the NLRome, and NRCs are scattered throughout the genome in gene clusters of varying complexities. Here, we describe NRCX, an atypical, but essential member of the NRC family that lacks canonical features of these NLR helper proteins, such as a functional N-terminal MADA motif and the capacity to trigger autoimmunity. In contrast to other NRCs, systemic gene silencing of NRCX markedly impairs plant growth resulting in a dwarf phenotype. Remarkably, dwarfism of NRCX silenced plants is partially dependent on NRCX paralogs NRC2 and NRC3, but not NRC4. Despite its negative impact on plant growth when silenced systemically, transient RNA interference of NRCX in mature N. benthamiana leaves doesnt result in visible cell death phenotypes. However, alteration of NRCX expression modulates the hypersensitive response mediated by NRC2 and NRC3 in a manner consistent with a negative role for NRCX in the NRC network. We conclude that NRCX is an atypical member of the NRC network that has evolved to contribute to the homeostasis of this genetically unlinked NLR network.
]]></description>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Duggan, C.</dc:creator>
<dc:creator>Bozkurt, T.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2021-11-15</dc:date>
<dc:identifier>doi:10.1101/2021.11.15.468391</dc:identifier>
<dc:title><![CDATA[An atypical NLR protein modulates the NRC immune receptor network]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-11-15</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.12.19.473371v1?rss=1">
<title>
<![CDATA[
A lineage-specific Exo70 is required for receptor kinase-mediated immunity in barley 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.12.19.473371v1?rss=1"
</link>
<description><![CDATA[
In the evolution of land plants, the plant immune system has experienced expansion in immune receptor and signaling pathways. Lineage-specific expansions have been observed in diverse gene families that are potentially involved in immunity, but lack causal association. Here, we show that Rps8-mediated resistance in barley to the fungal pathogen Puccinia striiformis f. sp. tritici (wheat stripe rust) is conferred by a genetic module: LRR-RK and Exo70FX12, which are together necessary and sufficient. The Rps8 LRR-RK is the ortholog of rice extracellular immune receptor Xa21 and Exo70FX12 is a member of the Poales-specific Exo70FX clade. The Exo70FX clade emerged after the divergence of the Bromeliaceae and Poaceae, and comprises from 2 to 75 members in sequenced grasses. These results demonstrate the requirement of a lineage-specific Exo70FX12 in Rps8 LRR-RK immunity and suggest that the Exo70FX clade may have evolved a specialized role in receptor kinase signaling.
]]></description>
<dc:creator>Holden, S.</dc:creator>
<dc:creator>Bergum, M.</dc:creator>
<dc:creator>Green, P.</dc:creator>
<dc:creator>Bettgenhaeuser, J.</dc:creator>
<dc:creator>Hernandez-Pinzon, I.</dc:creator>
<dc:creator>Thind, A.</dc:creator>
<dc:creator>Clare, S. J.</dc:creator>
<dc:creator>Russell, J. M.</dc:creator>
<dc:creator>Hubbard, A.</dc:creator>
<dc:creator>Taylor, J.</dc:creator>
<dc:creator>Smoker, M.</dc:creator>
<dc:creator>Gardiner, M.</dc:creator>
<dc:creator>Civolani, L.</dc:creator>
<dc:creator>Cosenza, F.</dc:creator>
<dc:creator>Rosignoli, S.</dc:creator>
<dc:creator>Strugala, R.</dc:creator>
<dc:creator>Molnar, I.</dc:creator>
<dc:creator>Simkova, H.</dc:creator>
<dc:creator>Dolezel, J.</dc:creator>
<dc:creator>Schaffrath, U.</dc:creator>
<dc:creator>Barrett, M.</dc:creator>
<dc:creator>Salvi, S.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:date>2021-12-21</dc:date>
<dc:identifier>doi:10.1101/2021.12.19.473371</dc:identifier>
<dc:title><![CDATA[A lineage-specific Exo70 is required for receptor kinase-mediated immunity in barley]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-12-21</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2021.12.28.474284v1?rss=1">
<title>
<![CDATA[
Clathrin-mediated Endocytosis Facilitates Internalization of Magnaporthe oryzae Effectors into Rice Cells 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2021.12.28.474284v1?rss=1"
</link>
<description><![CDATA[
Fungi and oomycetes deliver effectors into living plant cells to suppress defenses and control plant processes needed for infection. Little is known about the mechanism by which these pathogens translocate effector proteins across the plasma membrane into the plant cytoplasm. The blast fungus Magnaporthe oryzae secretes cytoplasmic effectors into a specialized biotrophic interfacial complex (BIC) before translocation. Here we show that cytoplasmic effectors within BICs are packaged into vesicles that are occasionally observed in the host cytoplasm. Live cell imaging with fluorescently-labeled rice showed that effector vesicles colocalize with plant plasma membrane and with clathrin light chain-1, a marker for clathrin-mediated endocytosis (CME). Inhibition of CME using Virus-Induced Gene Silencing (VIGS) and chemical treatments results in cytoplasmic effectors in swollen BICs lacking vesicles. In contrast, fluorescent marker co-localization, VIGS and chemical inhibitor studies failed to support a major role for clathrin-independent endocytosis in effector vesicle formation. Localization studies of two novel effectors, and of known effectors after CME inhibition, indicate that cytoplasmic effector translocation occurs underneath appressoria before invasive hyphal growth. Taken together, this study provides evidence that cytoplasmic effector translocation is mediated by clathrin-mediated endocytosis in BICs and suggests a role for M. oryzae effectors in co-opting plant endocytosis.
]]></description>
<dc:creator>Oliveira-Garcia, E.</dc:creator>
<dc:creator>Tamang, T. M.</dc:creator>
<dc:creator>Park, J.-E.</dc:creator>
<dc:creator>Dalby, M.</dc:creator>
<dc:creator>Martin-Urdiroz, M.</dc:creator>
<dc:creator>Rodriguez Herrero, C.</dc:creator>
<dc:creator>Hong Vu, A.</dc:creator>
<dc:creator>Park, S.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Valent, B.</dc:creator>
<dc:date>2021-12-29</dc:date>
<dc:identifier>doi:10.1101/2021.12.28.474284</dc:identifier>
<dc:title><![CDATA[Clathrin-mediated Endocytosis Facilitates Internalization of Magnaporthe oryzae Effectors into Rice Cells]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2021-12-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.01.03.474781v1?rss=1">
<title>
<![CDATA[
In planta transcriptomics reveals conflicts between pattern-triggered immunity and the AlgU sigma factor regulon 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.01.03.474781v1?rss=1"
</link>
<description><![CDATA[
In previous work, we determined the transcriptomic impacts of flg22 pre-induced Pattern Triggered Immunity (PTI) in Arabidopsis thaliana on the pathogen Pseudomonas syringae pv. tomato DC3000 (Pto). During PTI exposure we observed expression patterns in Pto reminiscent of those previously observed in a Pto algU mutant. AlgU is a conserved extracytoplasmic function sigma factor which has been observed to regulate over 950 genes in Pto in vitro. We sought to identify the AlgU regulon in planta.and which PTI-regulated genes overlapped with AlgU-regulated genes. In this study, we analyzed transcriptomic data from RNA-sequencing to identify the AlgU in planta regulon and its relationship with PTI. Our results showed that approximately 224 genes are induced by AlgU, while another 154 genes are downregulated by AlgU in Arabidopsis during early infection. Both stress response and virulence-associated genes were induced by AlgU, while the flagellar motility genes are downregulated by AlgU. Under the pre-induced PTI condition, more than half of these AlgU-regulated genes have lost induction/suppression in contrast to naive plants, and almost all function groups regulated by AlgU were affected by PTI.
]]></description>
<dc:creator>Wang, H.</dc:creator>
<dc:creator>Lovelace, A.</dc:creator>
<dc:creator>Smith, A.</dc:creator>
<dc:creator>Kvitko, B. H.</dc:creator>
<dc:date>2022-01-03</dc:date>
<dc:identifier>doi:10.1101/2022.01.03.474781</dc:identifier>
<dc:title><![CDATA[In planta transcriptomics reveals conflicts between pattern-triggered immunity and the AlgU sigma factor regulon]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-01-03</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.01.01.474684v1?rss=1">
<title>
<![CDATA[
Concerted expansion and contraction of immune receptor gene repertoires in plant genomes 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.01.01.474684v1?rss=1"
</link>
<description><![CDATA[
Recent reports suggest that cell-surface and intracellular immune receptors function synergistically to activate robust defence against pathogens, but whether or not they co-evolve is unclear. Here we determined the copy numbers of cell-surface and intracellular immune receptors in 208 species. Surprisingly, these receptor gene families contract and/or expand together in plant genomes, suggesting the mutual potentiation of immunity initiated by cell-surface and intracellular receptors is reflected in the concerted co-evolution of the size of their repertoires across plant species.
]]></description>
<dc:creator>Ngou, B. P. M.</dc:creator>
<dc:creator>Heal, R.</dc:creator>
<dc:creator>Wyler, M.</dc:creator>
<dc:creator>Schmid, M. W.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2022-01-02</dc:date>
<dc:identifier>doi:10.1101/2022.01.01.474684</dc:identifier>
<dc:title><![CDATA[Concerted expansion and contraction of immune receptor gene repertoires in plant genomes]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-01-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.01.27.478037v1?rss=1">
<title>
<![CDATA[
Arabidopsis CONSERVED BINDING OF EIF4E1 negatively regulates the NADPH oxidase RESPIRATORY BURST OXIDASE HOMOLOG D 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.01.27.478037v1?rss=1"
</link>
<description><![CDATA[
Cell-surface pattern recognition receptors sense invading pathogens by binding microbial or endogenous elicitors to activate plant immunity. These responses are under tight control to avoid excessive or untimely activation of cellular responses, which may otherwise be detrimental to host cells. How this fine-tuning is accomplished is an area of active study. We previously described a suppressor screen that identified Arabidopsis thaliana mutants with regained immune signaling in the immunodeficient genetic background bak1-5, which we named modifier of bak1-5 (mob) mutants. Here, we report that bak1-5 mob7 restores elicitor-induced signaling. Using a combination of map-based cloning and whole-genome resequencing, we identified MOB7 as CONSERVED BINDING OF EIF4E1 (CBE1), a plant-specific protein that interacts with highly-conserved eukaryotic translation initiation factor eIF4E1. Our data demonstrate that CBE1 regulate the accumulation of RESPIRATORY BURST OXIDASE HOMOLOG D (RBOHD), the NADPH oxidase responsible for elicitor-induced apoplast reactive oxygen species (ROS) production. Furthermore, several mRNA decapping and translation initiation factors co-localize with CBE1 and similarly regulate immune signaling. This study thus identifies a novel regulator of immune signaling and provides new insights into ROS regulation, and more generally translational control during plant stress responses.
]]></description>
<dc:creator>George, J.</dc:creator>
<dc:creator>Stegmann, M.</dc:creator>
<dc:creator>Monaghan, J.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2022-01-28</dc:date>
<dc:identifier>doi:10.1101/2022.01.27.478037</dc:identifier>
<dc:title><![CDATA[Arabidopsis CONSERVED BINDING OF EIF4E1 negatively regulates the NADPH oxidase RESPIRATORY BURST OXIDASE HOMOLOG D]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-01-28</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.01.27.477927v1?rss=1">
<title>
<![CDATA[
A wheat kinase and immune receptor form the host-specificity barrier against the blast fungus 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.01.27.477927v1?rss=1"
</link>
<description><![CDATA[
Since emerging in Brazil in 1985, wheat blast has spread throughout South America and recently appeared in Bangladesh and Zambia. We show that two wheat resistance genes, Rwt3 and Rwt4, acting as host-specificity barriers against non-Triticum blast pathotypes encode a nucleotide-binding leucine-rich repeat immune receptor and a tandem kinase, respectively. Molecular isolation of these genes allowed us to develop assays that will ensure the inclusion of these two genes in the wheat cultivars to forestall the recurrence of blast host jumps.
]]></description>
<dc:creator>Arora, S.</dc:creator>
<dc:creator>Steed, A.</dc:creator>
<dc:creator>Goddard, R.</dc:creator>
<dc:creator>Gaurav, K.</dc:creator>
<dc:creator>O'Hara, T.</dc:creator>
<dc:creator>Schoen, A.</dc:creator>
<dc:creator>Rawat, N.</dc:creator>
<dc:creator>Elkot, A. F.</dc:creator>
<dc:creator>Chinoy, C.</dc:creator>
<dc:creator>Nicholson, M. H.</dc:creator>
<dc:creator>Asuke, S.</dc:creator>
<dc:creator>Steuernagel, B.</dc:creator>
<dc:creator>Yu, G.</dc:creator>
<dc:creator>Awal, R.</dc:creator>
<dc:creator>Forner-Martinez, M.</dc:creator>
<dc:creator>Wingen, L.</dc:creator>
<dc:creator>Baggs, E.</dc:creator>
<dc:creator>Clarke, J.</dc:creator>
<dc:creator>Krasileva, K. V.</dc:creator>
<dc:creator>Tosa, Y.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:creator>Tiwari, V. K.</dc:creator>
<dc:creator>Wulff, B. B. H.</dc:creator>
<dc:creator>Nicholson, P.</dc:creator>
<dc:date>2022-01-28</dc:date>
<dc:identifier>doi:10.1101/2022.01.27.477927</dc:identifier>
<dc:title><![CDATA[A wheat kinase and immune receptor form the host-specificity barrier against the blast fungus]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-01-28</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.03.06.482794v1?rss=1">
<title>
<![CDATA[
SNP calling parameters have minimal impact on population structure and divergence time estimates for the rice blast fungus 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.03.06.482794v1?rss=1"
</link>
<description><![CDATA[
ObjectivesAccurate single-nucleotide polymorphisms (SNP) calls are crucial for robust evolutionary and population genetic inferences in genomic analyses. Such inferences can reveal the time-scales and processes associated with the emergence and spread of pandemic plant pathogens, such as the rice blast fungus Magnaporthe oryzae (Syn. Pyricularia oryzae). However, the specificity and sensitivity of SNP calls depend on the filtering parameters applied to the data. Here, we used a benchmarking approach to evaluate the impact of SNP calling on different population genetic analyses of the rice blast fungus, namely genetic clustering, topology of phylogenetic reconstructions and estimation of evolutionary rates.

ResultsTo benchmark SNP calling parameters, we generated a gold standard set of validated SNPs by sequencing nine M. oryzae genomes with both Illumina short-reads and Oxford Nanopore Technologies (ONT). We used the gold standard set of SNPs to identify the SNP calling parameter configuration that maximizes sensitivity and specificity. We found that the choice of parameter configurations can substantially change the number of ascertained SNPs, preferentially affecting SNPs segregating at low population frequency. However, SNP calling parameter configurations did not significantly affect the clustering of isolates in clonal lineages, the monophyly of each clonal lineage, and the estimation of evolutionary rates. We leverage the evolutionary rates obtained from each SNP calling parameter configuration to generate divergence time estimates that take into account the uncertainty associated with both the estimation of evolutionary rates and SNP calling. Our analysis indicates that M. oryzae clonal lineage expansions took place ~300 years ago.
]]></description>
<dc:creator>Latorre, S. M.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Malmgren, A.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Burbano, H. A.</dc:creator>
<dc:date>2022-03-07</dc:date>
<dc:identifier>doi:10.1101/2022.03.06.482794</dc:identifier>
<dc:title><![CDATA[SNP calling parameters have minimal impact on population structure and divergence time estimates for the rice blast fungus]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-03-07</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.04.25.489359v1?rss=1">
<title>
<![CDATA[
Effector-dependent activation and oligomerization of NRC helper NLRs by Rpi-amr3 and Rpi-amr1 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.04.25.489359v1?rss=1"
</link>
<description><![CDATA[
Plant pathogens compromise crop yields. Plants have evolved robust innate immunity that depends in part on intracellular Nucleotide-binding, Leucine Rich-Repeat (NLR) immune receptors that activate defense responses upon detection of pathogen-derived effectors. Most "sensor" NLRs that detect effectors require the activity of "helper" NLRs, but how helper NLRs support sensor NLR function is poorly understood. Many Solanaceae NLRs require the NRC (NLR-Required for Cell death) class of helper NLRs. We show here that Rpi-amr3, a sensor NLR from Solanum americanum, detects AVRamr3 from the potato late blight pathogen, Phytophthora infestans, and activates oligomerization of the helper NLR NRC2 into a high-molecular weight resistosome. The NRC2 resistosome also forms upon recognition of P. infestans effector AVRamr1 by another sensor NLR, Rpi-amr1. The ATP-binding motif of Rpi-amr3 is required for NRC2 resistosome formation, but not for interaction with the cognate effector. The NRC2 resistosome can be activated by AVRamr3 homologs from other Phytophthora species. Mechanistic understanding of NRC resistosome formation will underpin engineering crops with durable disease resistance.
]]></description>
<dc:creator>Ahn, H.-K.</dc:creator>
<dc:creator>Lin, X.</dc:creator>
<dc:creator>Olave-Achury, A. C.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2022-04-25</dc:date>
<dc:identifier>doi:10.1101/2022.04.25.489359</dc:identifier>
<dc:title><![CDATA[Effector-dependent activation and oligomerization of NRC helper NLRs by Rpi-amr3 and Rpi-amr1]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-04-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.04.25.489342v1?rss=1">
<title>
<![CDATA[
Sensor NLR immune proteins activate oligomerization of their NRC helper 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.04.25.489342v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding domain and leucine-rich repeat (NLR) immune receptors are important components of plant and metazoan innate immunity that can function as individual units or as pairs or networks. Upon activation, NLRs form multiprotein complexes termed resistosomes or inflammasomes. Whereas metazoan paired NLRs, such as NAIP/NLRC4, activate into hetero-complexes, the molecular mechanisms underpinning activation of plant paired NLRs, especially whether they associate in resistosome hetero-complexes is unknown. In asterid plant species, the NLR required for cell death (NRC) immune receptor network is composed of multiple resistance protein sensors and downstream helpers that confer immunity against diverse plant pathogens. Here, we show that pathogen effector-activation of the NLR proteins Rx (confers virus resistance) and Bs2 (confers bacterial resistance) leads to oligomerization of the helper NLR NRC2. Activated Rx does not oligomerize or enter into a stable complex with the NRC2 oligomer and remains cytoplasmic. In contrast, activated NRC2 oligomers accumulate in membrane-associated puncta. We propose an activation-and-release model for NLRs in the NRC immune receptor network. This points to a distinct activation model compared to mammalian paired NLRs.
]]></description>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Tumtas, Y.</dc:creator>
<dc:creator>Duggan, C.</dc:creator>
<dc:creator>Yuen, E. L. H.</dc:creator>
<dc:creator>Vergara Cruces, A.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Ahn, H.-K.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2022-04-25</dc:date>
<dc:identifier>doi:10.1101/2022.04.25.489342</dc:identifier>
<dc:title><![CDATA[Sensor NLR immune proteins activate oligomerization of their NRC helper]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-04-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.06.07.495176v1?rss=1">
<title>
<![CDATA[
Pangenomics facilitated with structural analysis reveals host NAD+ manipulation as a major virulence activity of bacterial effectors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.06.07.495176v1?rss=1"
</link>
<description><![CDATA[
Nicotinamide adenine dinucleotide (NAD+) has emerged as a key component in prokaryotic and eukaryotic immune systems and the recent discovery that Toll/interleukin-1 receptor (TIR) proteins function as NAD+ hydrolases (NADase) link NAD+-derived small molecules with immune signalling. We investigated pathogen manipulation of host NAD+ metabolism as a virulence strategy. Using the pangenome of the model bacterial pathogen Pseudomonas syringae, we conducted a structure-based similarity search from 35,000 orthogroups for type III effectors (T3Es) with potential NADase activity. Thirteen T3Es, including five newly identified candidates, were identified that possess domain(s) characteristic of seven NAD+-hydrolyzing enzyme families. Most P. syringae strains that depend on the Type III secretion system to cause disease, encode at least one NAD+-manipulating T3E, and many have several. We experimentally confirmed the type III-dependent secretion of a novel T3E, named HopBY, which shows structural similarity to both TIR and adenosine diphosphate ribose (ADPR) cyclase. Homologs of HopBY were predicted to be type VI effectors in diverse bacterial species, indicating potential recruitment of this activity by microbial proteins secreted during various interspecies interactions. HopBY efficiently hydrolyzes NAD+ and specifically produces 2cADPR, which can also be produced by TIR immune receptors of plants and other bacteria. Intriguingly, this effector promoted bacterial virulence, indicating that 2cADPR may not be the signalling molecule that directly initiates immunity. This study highlights a host-pathogen battle ground centred around NAD+ metabolism and provides insight into the NAD+-derived molecules involved in plant immunity.

Significance statementNAD+ metabolism plays a crucial role in plant and bacterial immunity. However, the diversity and scope of NAD+ processing steps in immune signalling remain unclear. Furthermore, whether pathogens can manipulate NAD+ metabolism to promote virulence is unknown. By conducting a pangenomic screen of the plant pathogen P. syringae, we found 13 type III effectors that potentially possess NADase activities, indicating that NAD+ manipulation is an important virulence mechanism. Further characterization of a newly identified effector HopBY showed that it produces a cyclic ADP-ribose isomer (2cADPR) and promotes bacterial infection and symptom development. This study clarifies the role of 2cADPR in immune signalling and provides an example of effectors as useful molecular probes to understand immunity.
]]></description>
<dc:creator>Hulin, M.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:date>2022-06-07</dc:date>
<dc:identifier>doi:10.1101/2022.06.07.495176</dc:identifier>
<dc:title><![CDATA[Pangenomics facilitated with structural analysis reveals host NAD+ manipulation as a major virulence activity of bacterial effectors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-06-07</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.06.06.494979v1?rss=1">
<title>
<![CDATA[
A pandemic clonal lineage of the wheat blast fungus 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.06.06.494979v1?rss=1"
</link>
<description><![CDATA[
Wheat, the most important food crop, is threatened by a blast disease pandemic. Here, we show that a clonal lineage of the wheat blast fungus recently spread to Asia and Africa following two independent introductions from South America. Through a combination of genome analyses and laboratory experiments, we show that the decade-old blast pandemic lineage can be controlled by the Rmg8 disease resistance gene and is sensitive to strobilurin fungicides. However, we also highlight the potential of the pandemic clone to evolve fungicide-insensitive variants and sexually recombine with African lineages. This underscores the urgent need for genomic surveillance to track and mitigate the spread of wheat blast outside of South America, and to guide pre-emptive wheat breeding for blast resistance.
]]></description>
<dc:creator>Latorre, S. M.</dc:creator>
<dc:creator>Were, V. M.</dc:creator>
<dc:creator>Foster, A. J.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Malmgren, A.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Asuke, S.</dc:creator>
<dc:creator>Reyes-Avila, S.</dc:creator>
<dc:creator>Gupta, D. R.</dc:creator>
<dc:creator>Jensen, C.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Mahmud, N. U.</dc:creator>
<dc:creator>Mehebub, S.</dc:creator>
<dc:creator>Mulenga, R. M.</dc:creator>
<dc:creator>Muzahid, A. N. M.</dc:creator>
<dc:creator>Paul, S.</dc:creator>
<dc:creator>Rabby, F. S. M.</dc:creator>
<dc:creator>Raha, A. A. M.</dc:creator>
<dc:creator>Ryder, L.</dc:creator>
<dc:creator>Shrestha, R.-K.</dc:creator>
<dc:creator>Sichilima, S.</dc:creator>
<dc:creator>Soanes, D. M.</dc:creator>
<dc:creator>Singh, P. K.</dc:creator>
<dc:creator>Bentley, A. R.</dc:creator>
<dc:creator>Saunders, D. G. O.</dc:creator>
<dc:creator>Tosa, Y.</dc:creator>
<dc:creator>Croll, D.</dc:creator>
<dc:creator>Lamour, K. H.</dc:creator>
<dc:creator>Islam, T.</dc:creator>
<dc:creator>Tembo, B.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Burbano, H. A.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2022-06-07</dc:date>
<dc:identifier>doi:10.1101/2022.06.06.494979</dc:identifier>
<dc:title><![CDATA[A pandemic clonal lineage of the wheat blast fungus]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-06-07</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.06.13.495685v1?rss=1">
<title>
<![CDATA[
The soybean rust pathogen Phakopsora pachyrhizi displays transposable element proliferation that correlates with broad host-range adaptation on legumes 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.06.13.495685v1?rss=1"
</link>
<description><![CDATA[
Asian soybean rust, caused by Phakopsora pachyrhizi, is one of the worlds most economically damaging agricultural diseases. Despite P. pachyrhizis impact, the exceptional size and complexity of its genome prevented generation of an accurate genome assembly. We simultaneously sequenced three P. pachyrhizi genomes uncovering a genome up to 1.25 Gb comprising two haplotypes with a transposable element (TE) content of ~93%. The proliferation of TEs within the genome occurred in several bursts and correlates with the radiation and speciation of the legumes. We present data of clear de-repression of TEs that mirrors expression of virulence-related candidate effectors. We can see a unique expansion in amino acid metabolism for this fungus. Our data shows that TEs play a dominant role in P. pachyrhizis genome and have a key impact on various processes such as host range adaptation, stress responses and genetic plasticity of the genome.
]]></description>
<dc:creator>Gupta, Y. K.</dc:creator>
<dc:creator>Marcelino-Guimaraes, F. C.</dc:creator>
<dc:creator>Lorrain, C.</dc:creator>
<dc:creator>Farmer, A. D.</dc:creator>
<dc:creator>Haridas, S.</dc:creator>
<dc:creator>Ferreira, E. G. C.</dc:creator>
<dc:creator>Lopes-Caitar, V. S.</dc:creator>
<dc:creator>Oliveira, L. S.</dc:creator>
<dc:creator>Morin, E.</dc:creator>
<dc:creator>Widdison, S.</dc:creator>
<dc:creator>Cameron, C.</dc:creator>
<dc:creator>Innoue, Y.</dc:creator>
<dc:creator>Thor, K.</dc:creator>
<dc:creator>Robinson, K.</dc:creator>
<dc:creator>Drula, E.</dc:creator>
<dc:creator>Henrissat, B.</dc:creator>
<dc:creator>LaButti, K.</dc:creator>
<dc:creator>Bini, A. M. R.</dc:creator>
<dc:creator>Paget, E.</dc:creator>
<dc:creator>Singan, V.</dc:creator>
<dc:creator>Daum, C.</dc:creator>
<dc:creator>Dorme, C.</dc:creator>
<dc:creator>van Hoek, M.</dc:creator>
<dc:creator>Janssen, A.</dc:creator>
<dc:creator>Chandat, L.</dc:creator>
<dc:creator>Tarriotte, Y.</dc:creator>
<dc:creator>Richardson, J.</dc:creator>
<dc:creator>Melo, B. d. V. A.</dc:creator>
<dc:creator>Wittenberg, A.</dc:creator>
<dc:creator>Schneiders, H.</dc:creator>
<dc:creator>Peyrard, S.</dc:creator>
<dc:creator>Zanardo, L. G.</dc:creator>
<dc:creator>Holtman, V. C.</dc:creator>
<dc:creator>Chauvel, F. C.</dc:creator>
<dc:creator>Link, T. I.</dc:creator>
<dc:creator>Balmer, D.</dc:creator>
<dc:creator>Müller, A. N.</dc:creator>
<dc:creator>Kind, S.</dc:creator>
<dc:creator>Bohnert, S.</dc:creator>
<dc:creator>Wirtz, L.</dc:creator>
<dc:creator>Chen, C.</dc:creator>
<dc:creator>Yan, M.</dc:creator>
<dc:creator>Ng, V.</dc:creator>
<dc:creator>G</dc:creator>
<dc:date>2022-06-13</dc:date>
<dc:identifier>doi:10.1101/2022.06.13.495685</dc:identifier>
<dc:title><![CDATA[The soybean rust pathogen Phakopsora pachyrhizi displays transposable element proliferation that correlates with broad host-range adaptation on legumes]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-06-13</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.06.16.496440v1?rss=1">
<title>
<![CDATA[
Oligomerisation of a plant helper NLR requires cell-surface and intracellular immune receptor activation 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.06.16.496440v1?rss=1"
</link>
<description><![CDATA[
Plant disease resistance involves both detection of microbial molecular patterns by cell-surface pattern recognition receptors and detection of pathogen effectors by intracellular NLR immune receptors. NLRs are classified as sensor NLRs, involved in effector detection, or helper NLRs required for sensor NLR signalling. TIR-domain-containing sensor NLRs (TNLs) require helper NLRs NRG1 and ADR1 for resistance, and their activation of defense also requires the lipase-domain proteins EDS1, SAG101 and PAD4. We investigated how the helper NLR NRG1 supports TNL-initiated immunity with EDS1 and SAG101. We find that NRG1 associates with EDS1 and SAG101 at the plasma membrane and in the nucleus, but only self-associates at the plasma membrane. Activation of TNLs is sufficient to trigger NRG1-EDS1-SAG101 interaction, but cell-surface receptor-initiated defense is also required to form an oligomeric Resistosome. The data point to formation of NRG1-EDS1-SAG101 heterotrimers in the nucleus upon intracellular receptor activation alone and indicate formation of NRG1-EDS1-SAG101 Resistosomes at the plasma membrane upon co-activation of intracellular and cell surface-receptor pathways.
]]></description>
<dc:creator>Feehan, J. M.</dc:creator>
<dc:creator>Wang, J.</dc:creator>
<dc:creator>Sun, X.</dc:creator>
<dc:creator>Choi, J.</dc:creator>
<dc:creator>Ahn, H.-K.</dc:creator>
<dc:creator>Ngou, B. P. M.</dc:creator>
<dc:creator>Parker, J. E.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2022-06-17</dc:date>
<dc:identifier>doi:10.1101/2022.06.16.496440</dc:identifier>
<dc:title><![CDATA[Oligomerisation of a plant helper NLR requires cell-surface and intracellular immune receptor activation]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-06-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.06.14.496076v1?rss=1">
<title>
<![CDATA[
Effector target-guided engineering of an integrated domain expands the disease resistance profile of a rice NLR immune receptor 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.06.14.496076v1?rss=1"
</link>
<description><![CDATA[
A subset of plant intracellular NLR immune receptors detect effector proteins, secreted by phytopathogens to promote infection, through unconventional integrated domains which resemble the effectors host targets. Direct binding of effectors to these integrated domains activates plant defences. The rice NLR receptor Pik-1 binds the Magnaporthe oryzae effector AVR-Pik through an integrated heavy metal-associated (HMA) domain. However, the stealthy alleles AVR-PikC and AVR-PikF avoid interaction with Pik-HMA and evade host defences. Here, we exploited knowledge of the biochemical interactions between AVR-Pik and its host target, OsHIPP19, to engineer novel Pik-1 variants that respond to AVR-PikC/F. First, we exchanged the HMA domain of Pikp-1 for OsHIPP19-HMA, demonstrating that effector targets can be incorporated into NLR receptors to provide novel recognition profiles. Second, we used the structure of OsHIPP19-HMA to guide mutagenesis of Pikp-HMA to expand its recognition profile. We demonstrate that the extended recognition profiles of engineered Pikp-1 variants correlate with effector binding in planta and in vitro, and with the gain of new contacts across the effector/HMA interface. Crucially, transgenic rice producing the engineered Pikp-1 variants were resistant to blast fungus isolates carrying AVR-PikC or AVR-PikF. These results demonstrate that effector target-guided engineering of NLR receptors can provide new-to- nature disease resistance in crops.

Graphical abstract

O_FIG O_LINKSMALLFIG WIDTH=186 HEIGHT=200 SRC="FIGDIR/small/496076v1_ufig1.gif" ALT="Figure 1">
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]]></description>
<dc:creator>Maidment, J. H.</dc:creator>
<dc:creator>Shimizu, M.</dc:creator>
<dc:creator>Vera, S.</dc:creator>
<dc:creator>Franceschetti, M.</dc:creator>
<dc:creator>Longya, A.</dc:creator>
<dc:creator>Stevenson, C. E.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Bialas, A.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2022-06-15</dc:date>
<dc:identifier>doi:10.1101/2022.06.14.496076</dc:identifier>
<dc:title><![CDATA[Effector target-guided engineering of an integrated domain expands the disease resistance profile of a rice NLR immune receptor]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-06-15</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.06.18.496527v1?rss=1">
<title>
<![CDATA[
Binding of a blast fungus Zinc-finger fold effector to a hydrophobic pocket in the host exocyst subunit Exo70 modulates immune recognition in rice 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.06.18.496527v1?rss=1"
</link>
<description><![CDATA[
Exocytosis plays an important role in plant-microbe interactions, both in pathogenesis and symbiosis. Exo70 proteins are integral components of the exocyst, an octameric complex that mediates tethering of vesicles to membranes in eukaryotes. Although plant Exo70s are known to be targeted by pathogen effectors, the underpinning molecular mechanisms and the impact of this interaction on infection is poorly understood. Here, we show the molecular basis of the association between the effector AVR- Pii of the blast fungus Maganaporthe oryzae and rice Exo70 alleles OsExo70F2 and OsExo70F3, which is sensed by the immune receptor pair Pii via an integrated RIN4/NOI domain. The crystal structure of AVR-Pii in complex with OsExo70F2 reveals that the effector binds to a conserved hydrophobic pocket in Exo70, defining a new effector/target binding interface. Structure-guided and random mutagenesis validates the importance of AVR-Pii residues at the Exo70 binding interface to sustain protein association and disease resistance in rice when challenged with fungal strains expressing effector mutants. Further, the structure of AVR-Pii defines a novel Zinc- finger effector fold (ZiF) distinct from the MAX fold previously described for the majority of characterized M. oryzae effectors. Our data suggests that blast fungus ZiF effectors bind a conserved Exo70 interface to manipulate plant exocytosis and that these effectors are also baited by plant immune receptors, pointing to new opportunities for engineering disease resistance.

Significance statementPlant diseases destroy [~]20-30% of annual crop production, contributing to global food insecurity. Discovering how pathogen effectors target host proteins to promote virulence is essential for understanding pathogenesis and can be used for developing disease resistant crops. Here, we reveal the structural basis of how an effector from the blast pathogen (AVR-Pii) binds a specific host target (rice Exo70), and how this underpins immune recognition. This has implications for understanding the molecular mechanisms of blast disease and for the engineering of new recognition specificities in plant immune receptors to confer resistance to a major crop pathogen.
]]></description>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Fujisaki, K.</dc:creator>
<dc:creator>Bentham, A. R.</dc:creator>
<dc:creator>Cruz Mireles, N.</dc:creator>
<dc:creator>Sanchez de Medina Hernandez, V.</dc:creator>
<dc:creator>Shimizu, M.</dc:creator>
<dc:creator>Lawson, D. M.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2022-06-19</dc:date>
<dc:identifier>doi:10.1101/2022.06.18.496527</dc:identifier>
<dc:title><![CDATA[Binding of a blast fungus Zinc-finger fold effector to a hydrophobic pocket in the host exocyst subunit Exo70 modulates immune recognition in rice]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-06-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.06.21.497003v1?rss=1">
<title>
<![CDATA[
The integrated LIM-peptidase domain of the CSA1/CHS3 paired immune receptor detects changes in DA1 family peptidase inhibitors to confer Albugo candida resistance in Arabidopsis. 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.06.21.497003v1?rss=1"
</link>
<description><![CDATA[
White blister rust, caused by the oomycete Albugo candida, is a widespread disease of Brassica crops. The Arabidopsis CSA1/DAR4 (also known as CSA1/CHS3) paired immune receptor carries an Integrated Domain (ID) with homology to the DA1 family of peptidases. Using domain swaps with DA1 family members, we show that the DAR4 ID acts as an integrated decoy for DAR3, which interacts with and inhibits the peptidase activities of DA1, DAR1 and DAR2 family members. Albugo infection rapidly lowered DAR3 levels and activates DA1 peptidase activity. This promotes endoreduplication of host tissues to support pathogen growth. We propose that DAR4/CSA1 senses the actions of a putative Albugo effector that reduces DAR3 levels and initiates defense.
]]></description>
<dc:creator>Gu, B.</dc:creator>
<dc:creator>Parkes, T.</dc:creator>
<dc:creator>Smith, C.</dc:creator>
<dc:creator>Lu, F.-H.</dc:creator>
<dc:creator>McKenzie, N.</dc:creator>
<dc:creator>Dong, H.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:creator>Cevik, V.</dc:creator>
<dc:creator>Bevan, M. W.</dc:creator>
<dc:date>2022-06-23</dc:date>
<dc:identifier>doi:10.1101/2022.06.21.497003</dc:identifier>
<dc:title><![CDATA[The integrated LIM-peptidase domain of the CSA1/CHS3 paired immune receptor detects changes in DA1 family peptidase inhibitors to confer Albugo candida resistance in Arabidopsis.]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-06-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.07.18.500532v1?rss=1">
<title>
<![CDATA[
The transcriptional landscape of plant infection by the rice blast fungus Magnaporthe oryzae reveals distinct families of temporally co-regulated and structurally conserved effectors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.07.18.500532v1?rss=1"
</link>
<description><![CDATA[
The rice blast fungus Magnaporthe oryzae causes a devastating disease which threatens global rice production. In spite of intense study, the biology of plant tissue invasion during blast disease remains poorly understood. Here we report a high resolution, transcriptional profiling study of the entire plant-associated development of the blast fungus. Our analysis revealed major temporal changes in fungal gene expression during plant infection. Pathogen gene expression could be classified into 10 modules of temporally co-expressed genes, providing evidence of induction of pronounced shifts in primary and secondary metabolism, cell signalling and transcriptional regulation. A set of 863 genes encoding secreted proteins are differentially expressed at specific stages of infection, and 546 were predicted to be effectors and named MEP (Magnaporthe effector protein) genes. Computational prediction of structurally-related MEPs, including the MAX effector family, revealed their temporal co-regulation in the same co-expression modules. We functionally characterised 32 MEP genes and demonstrate that Mep effectors are predominantly targeted to the cytoplasm of rice cells via the biotrophic interfacial complex (BIC), and use a common unconventional secretory pathway. Taken together, our study reveals major changes in gene expression associated with blast disease and identifies a diverse repertoire of effectors critical to successful infection.
]]></description>
<dc:creator>Yan, X.</dc:creator>
<dc:creator>Tang, B.</dc:creator>
<dc:creator>Ryder, L.</dc:creator>
<dc:creator>Maclean, D.</dc:creator>
<dc:creator>Were, V. M.</dc:creator>
<dc:creator>Eseola, A. B.</dc:creator>
<dc:creator>Cruz-Mireles, N.</dc:creator>
<dc:creator>Foster, A.</dc:creator>
<dc:creator>Oses-Ruiz, M.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:date>2022-07-19</dc:date>
<dc:identifier>doi:10.1101/2022.07.18.500532</dc:identifier>
<dc:title><![CDATA[The transcriptional landscape of plant infection by the rice blast fungus Magnaporthe oryzae reveals distinct families of temporally co-regulated and structurally conserved effectors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-07-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.07.19.500555v1?rss=1">
<title>
<![CDATA[
Tangled gene-for-gene interactions mediate co-evolution of the rice NLR immune receptor Pik and blast fungus effector proteins 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.07.19.500555v1?rss=1"
</link>
<description><![CDATA[
Studies focused solely on single organisms can fail to identify the networks underlying host-pathogen gene-for-gene interactions. Here, we integrate genetic analyses of rice (Oryza sativa, host) and rice blast fungus (Magnaporthe oryzae, pathogen) and uncover a new pathogen recognition specificity of the rice nucleotide-binding domain and leucine-rich repeat protein (NLR) immune receptor Pik, which mediates resistance to M. oryzae expressing the avirulence effector gene AVR-Pik. Rice Piks-1, encoded by an allele of Pik-1, recognizes a previously unidentified effector encoded by the M. oryzae avirulence gene AVR-Mgk1, which is found on a mini-chromosome. AVR-Mgk1 has no sequence similarity to known AVR-Pik effectors, and is prone to deletion from the mini-chromosome mediated by repeated Inago2 retrotransposon sequences. AVR-Mgk1 is detected by Piks-1 and by other Pik-1 alleles known to recognize AVR-Pik effectors; recognition is mediated by AVR-Mgk1 binding to the integrated heavy metal-associated (HMA) domain of Piks-1 and other Pik-1 alleles. Our findings highlight how complex gene-for-gene interaction networks can be disentangled by applying forward genetics approaches simultaneously to the host and pathogen. We demonstrate dynamic co-evolution between an NLR integrated domain and multiple families of effector proteins.
]]></description>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:creator>Abe, Y.</dc:creator>
<dc:creator>Takagi, H.</dc:creator>
<dc:creator>Abe, A.</dc:creator>
<dc:creator>Shimizu, M.</dc:creator>
<dc:creator>Ito, K.</dc:creator>
<dc:creator>Kanzaki, E.</dc:creator>
<dc:creator>Oikawa, K.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Bialas, A.</dc:creator>
<dc:creator>Ludke, D.</dc:creator>
<dc:creator>Chuma, I.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>Kobayashi, M.</dc:creator>
<dc:creator>Zheng, S.</dc:creator>
<dc:creator>Tosa, Y.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Fujisaki, K.</dc:creator>
<dc:date>2022-07-20</dc:date>
<dc:identifier>doi:10.1101/2022.07.19.500555</dc:identifier>
<dc:title><![CDATA[Tangled gene-for-gene interactions mediate co-evolution of the rice NLR immune receptor Pik and blast fungus effector proteins]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-07-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.08.11.503608v1?rss=1">
<title>
<![CDATA[
The Solanum americanum pangenome and effectoromics reveal new resistance genes against potato late blight 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.08.11.503608v1?rss=1"
</link>
<description><![CDATA[
Late blight caused by the oomycete pathogen Phytophthora infestans continues to cause major worldwide losses in potato and tomato. Most accessions of Solanum americanum, a globally distributed, wild Solanaceae plant, are highly resistant to late blight. We generated high-quality reference genomes of four S. americanum accessions, re-sequenced 52 accessions, and we defined variation in the NLR immune receptor genes (the S. americanum NLRome). We further screened for variation in recognition of [~]315 P. infestans RXLR effectors in 52 S. americanum accessions. Using these genotypic and phenotypic data, we cloned three novel NLR-encoding genes Rpi-amr4, Rpi-amr16 and Rpi-amr17, and determined their corresponding RXLR effector genes Avramr4 (PITG_22825), Avramr16 (PITG_02860) and Avramr17 (PITG_04373) from P. infestans. These genomic resources and methodology will support efforts to convert potato into a "nonhost" of late blight and can be applied to diseases of other crops.
]]></description>
<dc:creator>Lin, X.</dc:creator>
<dc:creator>Jia, Y.</dc:creator>
<dc:creator>Heal, R.</dc:creator>
<dc:creator>Prokchorchik, M.</dc:creator>
<dc:creator>Sindalovskaya, M.</dc:creator>
<dc:creator>Olave-Achury, A.</dc:creator>
<dc:creator>Makechemu, M.</dc:creator>
<dc:creator>Fairhead, S.</dc:creator>
<dc:creator>Noureen, A.</dc:creator>
<dc:creator>Heo, J.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Smoker, M.</dc:creator>
<dc:creator>Taylor, J.</dc:creator>
<dc:creator>Shrestha, R.-K.</dc:creator>
<dc:creator>Lee, Y. Y.</dc:creator>
<dc:creator>Zhang, C.</dc:creator>
<dc:creator>Park, S. J.</dc:creator>
<dc:creator>sohn, k. h.</dc:creator>
<dc:creator>Huang, S.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2022-08-11</dc:date>
<dc:identifier>doi:10.1101/2022.08.11.503608</dc:identifier>
<dc:title><![CDATA[The Solanum americanum pangenome and effectoromics reveal new resistance genes against potato late blight]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-08-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.08.29.505667v1?rss=1">
<title>
<![CDATA[
Wild grass isolates of Magnaporthe (Syn. Pyricularia) spp. from Germany can cause blast disease on cereal crops 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.08.29.505667v1?rss=1"
</link>
<description><![CDATA[
Pathogens that cause destructive crop diseases often infect wild host plants. However, surveys of major plant pathogens tend to be skewed towards cultivated crops and often neglect the wild hosts. Here, we report an emerging disease threat generated by the blast fungus Magnaporthe (Syn. Pyricularia) spp. in central Europe. We found that this notoriously devastating plant pathogen infects the wild grasses foxtail millet (Setaria spp.) and crabgrass (Digitaria spp.) in south-western Germany, a region previously deemed unfavorable for blast disease. Using phenotypic characterization and genomic analyses, we determined that the observed disease symptoms are associated with the Setaria spp.-infecting lineage of M. oryzae and its sister species Magnaporthe grisea. We showed that M. oryzae isolates can infect barley and wheat, thus highlighting the risk of pathogen spread to crops. In addition, M. oryzae isolates which co-occur in natural populations display compatible mating types and variable candidate effector gene content, which may enhance the pathogens adaptive potential. Our findings stress the risk of blast fungus infections expanding into European cereal crops through migration and host jumps. This underlines the importance for pathogen surveillance not only on cultivated crops, but also on wild host plants.

Author SummaryWild plant species are often overlooked during pathogen virulence surveys. However, many of the diseases we observe in crops are a consequence of host jumps from wild to cultivated plant species. This is reminiscent of zoonotic diseases, where host jumps from wild animals to humans result in new disease outbreaks. Here, we report that the notoriously devastating blast fungus Magnaporthe (Syn. Pyricularia) spp. occurs on wild grasses in south-western Germany. This region, which is at the center of the European cereal belt, has so far been viewed as having unfavorable climatic conditions for the blast disease. The newly identified blast fungus isolates have the capacity to infect wheat and barley cultivars, highlighting the risk of the disease spreading to staple cereal crops. In addition, there is potential for sexual recombination in local populations, which may increase the evolutionary potential of the fungus and might facilitate host jumps to cereal crops. Our findings emphasize the urgent need for surveillance of plant diseases on both wild hosts and crops.
]]></description>
<dc:creator>Barragan, A. C.</dc:creator>
<dc:creator>Latorre, S. M.</dc:creator>
<dc:creator>Mock, P. G.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Malmgren, A.</dc:creator>
<dc:creator>Burbano, H. A.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:date>2022-08-29</dc:date>
<dc:identifier>doi:10.1101/2022.08.29.505667</dc:identifier>
<dc:title><![CDATA[Wild grass isolates of Magnaporthe (Syn. Pyricularia) spp. from Germany can cause blast disease on cereal crops]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-08-29</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.08.30.505899v1?rss=1">
<title>
<![CDATA[
Direct measurement of appressorium turgor using a molecular mechanosensor in the rice blast fungus Magnaporthe oryzae 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.08.30.505899v1?rss=1"
</link>
<description><![CDATA[
Many plant pathogenic fungi forcibly enter their hosts to cause disease. The rice blast fungus Magnaporthe oryzae, for example, infects plants using a specialised infection cell called an appressorium, which generates enormous turgor to drive a rigid penetration peg through the rice leaf cuticle. While these vast internal pressures are a critical weapon in fungal host penetration, they have remained very challenging to probe directly during host invasion, leaving our understanding of these extreme cellular mechanics incomplete. Here, we combine Fluorescence Lifetime Imaging (FLIM) with a membrane-targeting molecular mechanoprobe to quantify changes in membrane tension as a direct proxy for appressorial turgor in M. oryzae. We report that mature melanin-pigmented M. oryzae appressoria display a heterogeneous low fluorescence lifetime and high membrane tension, consistent with enormous turgor. These extreme pressures lead to large-scale spatial heterogeneities in membrane mechanics, much greater than observed in any other cell type previously, highlighting the extreme mechanics of turgor-driven appressorium-mediated plant infection. By contrast, appressoria of non-pathogenic melanin-deficient mutants, alb1 and buf1, or immature non-melanised appressoria, exhibit high fluorescence lifetime, consistent with low membrane tension and turgor, that remain spatially homogeneous. To evaluate the method, we investigated turgor dynamics in a range of mutants impaired in appressorium function. We show that the turgor sensor kinase mutant{Delta} sln1, recently proposed to generate excess appressorium turgor, displayed a significantly higher membrane tension compared to an isogenic wild type M. oryzae strain. This non-invasive, live cell imaging technique allows direct quantification and visualization of the enormous turgor pressures deployed during pathogen infection.
]]></description>
<dc:creator>Ryder, L. S.</dc:creator>
<dc:creator>Lopez, S. G.</dc:creator>
<dc:creator>Michels, L.</dc:creator>
<dc:creator>Eseola, A. B.</dc:creator>
<dc:creator>Sprakel, J.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:date>2022-08-31</dc:date>
<dc:identifier>doi:10.1101/2022.08.30.505899</dc:identifier>
<dc:title><![CDATA[Direct measurement of appressorium turgor using a molecular mechanosensor in the rice blast fungus Magnaporthe oryzae]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-08-31</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.09.04.506535v1?rss=1">
<title>
<![CDATA[
Rgs1 is a regulator of effector gene expression during plant infection by the rice blast fungus Magnaporthe oryzae 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.09.04.506535v1?rss=1"
</link>
<description><![CDATA[
To cause rice blast disease the filamentous fungus Magnaporthe oryzae secretes a battery of effector proteins into host plant tissue to facilitate infection. Effector-encoding genes are expressed only during plant infection and show very low expression during other developmental stages. How effector gene expression is regulated in such a precise manner during invasive growth by M. oryzae is not known. Here, we report a forward-genetic screen to identify regulators of effector gene expression, based on selection of mutants that show constitutive effector gene expression. Using this simple screen, we identify Rgs1, a regulator of G-protein signalling (RGS) protein that is necessary for appressorium development, as a novel transcriptional regulator of effector gene expression, which acts prior to plant infection. We show that an N-terminal domain of Rgs1, possessing transactivation activity, is required for effector gene regulation and acts in an RGS-independent manner. Rgs1 controls expression of at least 60 temporally co-regulated effector genes, preventing their transcription during the pre-penetration stage of development prior to plant infection. A regulator of appressorium morphogenesis is therefore also required for orchestration of pathogen gene expression required for invasive growth by M. oryzae during plant infection.
]]></description>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Tang, B.</dc:creator>
<dc:creator>Yan, X.</dc:creator>
<dc:creator>Ryder, L. S.</dc:creator>
<dc:creator>Cruz-Mireles, N.</dc:creator>
<dc:creator>Soanes, D. M.</dc:creator>
<dc:creator>Molinari, C.</dc:creator>
<dc:creator>Foster, A. J.</dc:creator>
<dc:date>2022-09-05</dc:date>
<dc:identifier>doi:10.1101/2022.09.04.506535</dc:identifier>
<dc:title><![CDATA[Rgs1 is a regulator of effector gene expression during plant infection by the rice blast fungus Magnaporthe oryzae]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-09-05</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.10.10.511592v1?rss=1">
<title>
<![CDATA[
Allelic compatibility in plant immune receptors facilitates engineering of new effector recognition specificities. 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.10.10.511592v1?rss=1"
</link>
<description><![CDATA[
Engineering expanded effector recognition in plant immune receptors is a promising prospect for generating new disease resistant crop varieties. However, modification of plant NLR receptors has proven challenging due to the lack of understanding of their context as part of complex immune systems. Here, we demonstrate a new avenue for NLR-mediated engineering that exploits the allelic diversity in the Pik NLR pair to allow for the generation of receptors with expanded recognition specificities, which would otherwise result in constitutive cell death. This work lays the foundation for the incorporation of new effector recognition motifs into the Pik system and advances the development of designer NLRs that can be tailored to specific secreted pathogen signatures.

AbstractEngineering the plant immune system offers genetic solutions to mitigate crop diseases caused by diverse agriculturally significant pathogens and pests. Modification of intracellular plant immune receptors of the nucleotide-binding leucine rich repeat (NLRs) superfamily for expanded recognition of pathogen virulence proteins (effectors) is a promising approach for engineering novel disease resistance. However, engineering can cause NLR autoactivation, resulting in constitutive defence responses that are deleterious to the plant. This may be due to plant NLRs associating in highly complex signalling networks that co-evolve together, and changes through breeding or genetic modification can generate incompatible combinations, resulting in autoimmune phenotypes. We have previously shown how alleles of the rice NLR pair Pik have differentially co-evolved, and how sensor/helper mismatching between non-co-evolved alleles triggers constitutive activation and cell death (De la Concepcion et al., 2021b). Here, we dissect incompatibility determinants in the Pik pair and found that HMA domains integrated in Pik-1 not only evolved to bind pathogen effectors but also likely co-evolved with other NLR domains to maintain immune homeostasis. This explains why changes in integrated domains can lead to autoactivation. We then used this knowledge to facilitate engineering of new effector recognition specificities overcoming initial autoimmune penalties. We show that by mismatching alleles of the rice sensor and helper NLRs Pik-1 and Pik-2, we can enable the integration of synthetic HMA domains with novel and enhanced recognition of an effector from the rice blast fungus. Taken together, our results reveal a new strategy for engineering NLRs, which has the potential to allow an expanded set of integrations and therefore new disease resistance specificities in plants.
]]></description>
<dc:creator>Bentham, A. R.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Benjumea, J. V.</dc:creator>
<dc:creator>Jones, S.</dc:creator>
<dc:creator>Mendel, M.</dc:creator>
<dc:creator>Stubbs, J.</dc:creator>
<dc:creator>Stevenson, C. E.</dc:creator>
<dc:creator>Maidment, J. H.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Zdrzalek, R.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2022-10-11</dc:date>
<dc:identifier>doi:10.1101/2022.10.10.511592</dc:identifier>
<dc:title><![CDATA[Allelic compatibility in plant immune receptors facilitates engineering of new effector recognition specificities.]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-10-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.10.19.512840v1?rss=1">
<title>
<![CDATA[
The N-terminal executioner domains of NLR immune receptors are functionally conserved across major plant lineages 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.10.19.512840v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding domain and leucine-rich repeat (NLR) proteins are a prominent class of intracellular immune receptors that are present across diverse plant lineages. However, our understanding of plant NLR structure and function is limited to the evolutionarily young flowering plant clade (angiosperms). Here, we describe an extended spectrum of NLR diversity across major plant lineages and demonstrate functional conservation of N-terminal  executioner domains that trigger immune responses. We show that broadly distributed CC (coiled-coil) and TIR (toll/interleukin-1 receptor) domains retain executioner function through trans-lineage activation of immune-related cell death in the model angiosperm Nicotiana benthamiana. Further examination of a CC subfamily specific to non-flowering lineages uncovered an essential N-terminal MAEPL motif with functional similarity to resistosome-forming CC-NLRs. Ectopic activation of the MAEPL-type CC in the divergent liverwort Marchantia polymorpha led to profound growth inhibition, defense gene activation, and signatures of cell death resembling CC activity in flowering plants. Moreover, comparative macroevolutionary transcriptomics in Marchantia and Nicotiana identified conserved CC responsive genes, providing further insight into the core aspects of CC function shared between flowering and non-flowering plants. Our findings highlight the need to understand NLR structure and function across the full spectrum of plant diversity.
]]></description>
<dc:creator>Chia, K.-S.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Vickers, M.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Carella, P.</dc:creator>
<dc:date>2022-10-19</dc:date>
<dc:identifier>doi:10.1101/2022.10.19.512840</dc:identifier>
<dc:title><![CDATA[The N-terminal executioner domains of NLR immune receptors are functionally conserved across major plant lineages]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-10-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.10.21.512921v1?rss=1">
<title>
<![CDATA[
Barley MLA3 recognizes the host-specificity determinant PWL2 from rice blast (M. oryzae) 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.10.21.512921v1?rss=1"
</link>
<description><![CDATA[
Plant nucleotide-binding leucine-rich repeat immune receptors (NLRs) directly or indirectly recognize pathogen-secreted effector molecules to initiate plant defense. Recognition of multiple pathogens by a single NLR is rare and usually occurs via monitoring for changes to host proteins; few characterized NLRs have been shown to recognize multiple effectors. The barley NLR Mla has undergone functional diversification and Mla alleles recognize host-adapted isolates of barley powdery mildew (Blumeria graminis f. sp. hordei; Bgh). Here, we show that Mla3 also confers resistance to rice blast (Magnaporthe oryzae) in a dosage dependent manner. Using a forward genetic screen, we discovered that the recognized effector from M. oryzae is PWL2, a host range determinant factor that prevents M. oryzae from infecting weeping lovegrass (Eragrostis curvula). Mla3 has therefore convergently evolved the capacity to recognize effectors from diverse pathogens.
]]></description>
<dc:creator>Brabham, H. J.</dc:creator>
<dc:creator>Gomez De La Cruz, D.</dc:creator>
<dc:creator>Were, V.</dc:creator>
<dc:creator>Shimizu, M.</dc:creator>
<dc:creator>Saitoh, H.</dc:creator>
<dc:creator>Hernandez-Pinzon, I.</dc:creator>
<dc:creator>Green, P.</dc:creator>
<dc:creator>Lorang, J.</dc:creator>
<dc:creator>Fujisaki, K.</dc:creator>
<dc:creator>Sato, K.</dc:creator>
<dc:creator>Molnar, I.</dc:creator>
<dc:creator>Simkova, H.</dc:creator>
<dc:creator>Dolezel, J.</dc:creator>
<dc:creator>Russell, J.</dc:creator>
<dc:creator>Taylor, J.</dc:creator>
<dc:creator>Smoker, M.</dc:creator>
<dc:creator>Gupta, Y. K.</dc:creator>
<dc:creator>Wolpert, T.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:date>2022-10-22</dc:date>
<dc:identifier>doi:10.1101/2022.10.21.512921</dc:identifier>
<dc:title><![CDATA[Barley MLA3 recognizes the host-specificity determinant PWL2 from rice blast (M. oryzae)]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-10-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.12.05.519081v1?rss=1">
<title>
<![CDATA[
Extensive immune receptor repertoire diversity in disease-resistant rice landraces 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.12.05.519081v1?rss=1"
</link>
<description><![CDATA[
Plants have powerful defence mechanisms, and extensive immune receptor repertoires, yet crop monocultures are prone to epidemic diseases. Rice is susceptible to many diseases, such as rice blast caused by Magnaporthe oryzae. Varietal resistance of rice to blast relies on intracellular nucleotide binding, leucine-rich repeat (NLR) receptors that recognize specific pathogen molecules and trigger immune responses. In the Yuanyang terraces in south-west China, rice landraces rarely show severe losses to disease whereas commercial inbred lines show pronounced field susceptibility. Here, we investigate within-landrace NLR sequence diversity of nine rice landraces and eleven modern varieties of indica, japonica and aus using complexity reduction techniques. We find that NLRs display high sequence diversity in landraces, consistent with balancing selection, and that balancing selection at NLRs is more pervasive in landraces than modern varieties. Notably, modern varieties lack many ancient NLR haplotypes that are retained in some landraces. Our study emphasises the value of standing genetic variation that is maintained in farmer landraces as resource to make modern crops and agroecosystems less prone to disease.
]]></description>
<dc:creator>Gladieux, P.</dc:creator>
<dc:creator>van Oosterhout, C.</dc:creator>
<dc:creator>Fairhead, S.</dc:creator>
<dc:creator>Jouet, A.</dc:creator>
<dc:creator>Ortiz, D.</dc:creator>
<dc:creator>Ravel, S.</dc:creator>
<dc:creator>Shrestha, R.-K.</dc:creator>
<dc:creator>Frouin, J.</dc:creator>
<dc:creator>He, X.</dc:creator>
<dc:creator>Zhu, Y.</dc:creator>
<dc:creator>Morel, J. B.</dc:creator>
<dc:creator>Huang, H.</dc:creator>
<dc:creator>Kroj, T.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2022-12-08</dc:date>
<dc:identifier>doi:10.1101/2022.12.05.519081</dc:identifier>
<dc:title><![CDATA[Extensive immune receptor repertoire diversity in disease-resistant rice landraces]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-12-08</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2022.12.11.519957v1?rss=1">
<title>
<![CDATA[
Resurrection of plant disease resistance proteins via helper NLR bioengineering 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2022.12.11.519957v1?rss=1"
</link>
<description><![CDATA[
Parasites counteract host immunity by suppressing helper NLR proteins that function as central nodes in immune receptor networks. Understanding the mechanisms of immunosuppression can lead to strategies for bioengineering disease resistance. Here, we show that a cyst nematode virulence effector binds and inhibits oligomerization of the helper NLR protein NRC2 by physically preventing intramolecular rearrangements required for activation. A single amino acid polymorphism at the binding interface between NRC2 and the inhibitor is sufficient for this helper NLR to evade immune suppression, thereby restoring the activity of multiple disease resistance genes. This points to a novel strategy for resurrecting disease resistance in crop genomes.

One sentence summaryA helper NLR is mutated to evade inhibition by a parasite effector.
]]></description>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Selvaraj, M.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Lawson, D. M.</dc:creator>
<dc:creator>Tumtas, Y.</dc:creator>
<dc:creator>Duggan, C.</dc:creator>
<dc:creator>Yuen, E. L. H.</dc:creator>
<dc:creator>Stevenson, C. E. M.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:date>2022-12-11</dc:date>
<dc:identifier>doi:10.1101/2022.12.11.519957</dc:identifier>
<dc:title><![CDATA[Resurrection of plant disease resistance proteins via helper NLR bioengineering]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2022-12-11</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.01.17.524393v1?rss=1">
<title>
<![CDATA[
Inducible TRAP RNA profiling reveals host genes expressed in Arabidopsis cells haustoriated by downy mildew 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.01.17.524393v1?rss=1"
</link>
<description><![CDATA[
The downy mildew oomycete Hyaloperonospora arabidopsidis, an obligate filamentous pathogen, infects Arabidopsis by forming feeding structures called haustoria inside host cells. Previous transcriptome analyses revealed host genes are specifically induced during infection; however, RNA profiling from infected tissues may fail to capture key transcriptional events occurring exclusively in haustoriated host cells where the pathogen injects virulence effectors to modulate host immunity. To determine interactions between Arabidopsis and H. arabidopsidis at the cellular level, we devised a new translating ribosome affinity purification system applicable to inducible, including pathogen-responsive, promoters thus enabling haustoriated cell-specific RNA profiling. Among the host genes specifically expressed in H. arabidopsidis-haustoriated cells, we found genes that promote either susceptibility or resistance to the pathogen, providing new insights into the Arabidopsis/downy mildew interaction. We propose that our novel protocol for profiling cell-specific transcripts will be applicable to several stimulus-specific contexts and other plant-pathogen interactions.
]]></description>
<dc:creator>Asai, S.</dc:creator>
<dc:creator>Cevik, V.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:creator>Shirasu, K.</dc:creator>
<dc:date>2023-01-20</dc:date>
<dc:identifier>doi:10.1101/2023.01.17.524393</dc:identifier>
<dc:title><![CDATA[Inducible TRAP RNA profiling reveals host genes expressed in Arabidopsis cells haustoriated by downy mildew]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-01-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.02.02.524463v1?rss=1">
<title>
<![CDATA[
Evidence for a core set of microbial lichen symbionts from a global survey of metagenomes 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.02.02.524463v1?rss=1"
</link>
<description><![CDATA[
Lichens are the archetypal symbiosis and the one for which the term was coined. Although application of shotgun sequencing techniques has shown that many lichen symbioses can harbour more symbionts than the canonically recognized fungus and photobiont, no global census of lichen organismal composition has been undertaken. Here, we analyze the genome content of 437 lichen metagenomes from six continents, and show that four bacterial lineages occur in the majority of lichen symbioses, at a frequency on par with algal photobionts. A single bacterial genus, Lichenihabitans, occurs in nearly one-third of all lichens sampled. Genome annotations from the most common lichen bacterial symbionts suggest they are aerobic anoxygenic photoheterotrophs and produce essential vitamins, but do not fix nitrogen. We also detected secondary basidiomycete symbionts in about two-thirds of analyzed metagenomes. Our survey suggests a core set of four to seven microbial symbionts are involved in forming and maintaining lichen symbioses.
]]></description>
<dc:creator>Tagirdzhanova, G.</dc:creator>
<dc:creator>Saary, P.</dc:creator>
<dc:creator>Cameron, E. S.</dc:creator>
<dc:creator>Garber, A.</dc:creator>
<dc:creator>Diaz Escandon, D.</dc:creator>
<dc:creator>Goyette, S.</dc:creator>
<dc:creator>Tuovinen Nogerius, V.</dc:creator>
<dc:creator>Passo, A.</dc:creator>
<dc:creator>Mayrhofer, H.</dc:creator>
<dc:creator>Holien, H.</dc:creator>
<dc:creator>Tonsberg, T.</dc:creator>
<dc:creator>Stein, L. Y.</dc:creator>
<dc:creator>Finn, R. D.</dc:creator>
<dc:creator>Spribille, T.</dc:creator>
<dc:date>2023-02-02</dc:date>
<dc:identifier>doi:10.1101/2023.02.02.524463</dc:identifier>
<dc:title><![CDATA[Evidence for a core set of microbial lichen symbionts from a global survey of metagenomes]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-02-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.03.19.533321v1?rss=1">
<title>
<![CDATA[
Seed Longevity is Controlled by Metacaspases 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.03.19.533321v1?rss=1"
</link>
<description><![CDATA[
To survive extreme desiccation, seeds enter dormancy that can last millennia. This dormancy involves the accumulation of protective but structurally disordered storage proteins through unknown adjustments of proteolytic surveillance mechanisms. Mutation of all six types II metacaspases (MCAs)-II in the model plant Arabidopsis revealed their essential role in modulating these proteolytic mechanisms. MCA-II mutant seeds fail to properly target at the endoplasmic reticulum (ER) the AAA ATPase Cell Division Cycle 48 (CDC48) to dispose of misfolded proteins. MCA-IIs cleave a CDC48 adaptor, the ubiquitination regulatory X domain-containing (PUX) responsible for localizing CDC48 to the lipid droplets. When cleaved, CDC48-PUX is inactivated and allows a lipid droplet-to-ER shuttling of CDC48, an important step in the regulation of seeds lifespan. In sum, we uncover antagonism between proteolytic pathways bestowing longevity.

One-Sentence SummaryMetacaspase proteases confer seed longevity by antagonizing CDC48 activity.
]]></description>
<dc:creator>Liu, C.</dc:creator>
<dc:creator>Hatzianestis, I. H.</dc:creator>
<dc:creator>Pfirrmann, T.</dc:creator>
<dc:creator>Reza, S. H.</dc:creator>
<dc:creator>Minina, A. A.</dc:creator>
<dc:creator>Moazzami, A.</dc:creator>
<dc:creator>Stael, S.</dc:creator>
<dc:creator>Gutierez-Beltran, E.</dc:creator>
<dc:creator>Pitsili, E.</dc:creator>
<dc:creator>Doermann, P.</dc:creator>
<dc:creator>D Andrea, S.</dc:creator>
<dc:creator>Gevaert, K.</dc:creator>
<dc:creator>Romero-Campero, F.</dc:creator>
<dc:creator>Ting, P.</dc:creator>
<dc:creator>Nowack, M. K.</dc:creator>
<dc:creator>Van Breusegem, F.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Bozhkov, P. V.</dc:creator>
<dc:creator>Moschou, P. N.</dc:creator>
<dc:date>2023-03-20</dc:date>
<dc:identifier>doi:10.1101/2023.03.19.533321</dc:identifier>
<dc:title><![CDATA[Seed Longevity is Controlled by Metacaspases]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-03-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.03.23.533910v1?rss=1">
<title>
<![CDATA[
The immune receptor SNC1 monitors helper NLRs targeted by a bacterial effector 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.03.23.533910v1?rss=1"
</link>
<description><![CDATA[
Plants deploy intracellular receptors to counteract pathogen effectors that suppress cell-surface receptor-mediated immunity. To what extent pathogens manipulate also immunity mediated by intracellular receptors, and how plants tackle such manipulation, remains unknown. Arabidopsis thaliana encodes three very similar ADR1 class helper NLRs (ADR1, ADR1-L1 and ADR1-L2), which play key roles in plant immunity initiated by intracellular receptors. Here, we report that Pseudomonas syringae AvrPtoB, an effector with E3 ligase activity, can suppress ADR1-L1- and ADR1-L2-mediated cell death. ADR1, however, evades such suppression by diversification of two ubiquitination sites targeted by AvrPtoB. The intracellular sensor NLR SNC1 interacts with and guards the CCR domains of ADR1-L1 and ADR-L2. Removal of ADR1-L1 and ADR1-L2 or delivery of AvrPtoB activates SNC1, which then signals through ADR1 to trigger immunity. Our work not only uncovers the long sought-after physiological function of SNC1 in pathogen defense, but also that reveals how plants can use dual strategies, sequence diversification and a multiple layered guard-guardee system, to counteract pathogen attack on core immunity functions.
]]></description>
<dc:creator>Wang, M.</dc:creator>
<dc:creator>Chen, J.</dc:creator>
<dc:creator>Wu, R.</dc:creator>
<dc:creator>Guo, H.</dc:creator>
<dc:creator>Chen, Y.</dc:creator>
<dc:creator>Li, Z.</dc:creator>
<dc:creator>Wei, L.</dc:creator>
<dc:creator>Liu, C.</dc:creator>
<dc:creator>He, S.</dc:creator>
<dc:creator>Du, M.</dc:creator>
<dc:creator>Guo, Y.</dc:creator>
<dc:creator>Peng, Y.-L.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Weigel, D.</dc:creator>
<dc:creator>Huang, J.</dc:creator>
<dc:creator>Zhu, W.</dc:creator>
<dc:date>2023-03-24</dc:date>
<dc:identifier>doi:10.1101/2023.03.23.533910</dc:identifier>
<dc:title><![CDATA[The immune receptor SNC1 monitors helper NLRs targeted by a bacterial effector]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-03-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.04.03.535386v1?rss=1">
<title>
<![CDATA[
Cell type-specific responses to fungal infection in plants revealed by single-cell transcriptomics 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.04.03.535386v1?rss=1"
</link>
<description><![CDATA[
Plant infection by microbial pathogens is a dynamic process. Here, we investigated the heterogeneity of plant responses in the context of pathogen location. A single-cell atlas of Arabidopsis thaliana leaves challenged by the fungus Colletotrichum higginsianum revealed cell type-specific gene expression that highlights an enrichment of intracellular immune receptors in vasculature cells. Using trajectory inference, we assigned cells that directly interacted with the invasive hyphae. Further analysis of cells at these infection sites revealed transcriptional plasticity based on cell type. A reprogramming of abscisic acid signalling was specifically activated in guard cells. Consistently, a contact-dependent stomatal closure was observed, possibly representing a defense response that anticipates pathogen invasive growth. We defined cell type-specific deployments of genes activating indole glucosinolate biosynthesis at the infection sites, and determined their contribution to resistance. This research highlights the spatial dynamics of plant response during infection and reveals cell type-specific processes and gene functions.
]]></description>
<dc:creator>Tang, B.</dc:creator>
<dc:creator>Feng, L.</dc:creator>
<dc:creator>Ding, P.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:date>2023-04-04</dc:date>
<dc:identifier>doi:10.1101/2023.04.03.535386</dc:identifier>
<dc:title><![CDATA[Cell type-specific responses to fungal infection in plants revealed by single-cell transcriptomics]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-04-04</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.04.12.536646v1?rss=1">
<title>
<![CDATA[
A GH81-type β-glucan-binding protein facilitates colonization by mutualistic fungi in barley 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.04.12.536646v1?rss=1"
</link>
<description><![CDATA[
Cell walls are important interfaces of plant-fungal interactions. Host cell walls act as robust physical and chemical barriers against fungal invaders, making them an essential line of defense. Upon fungal colonization, plants deposit phenolics and callose at the sites of fungal penetration to reinforce their walls and prevent further fungal progression. Alterations in the composition of plant cell walls significantly impact host susceptibility. Furthermore, plants and fungi secrete glycan hydrolases acting on each others cell walls. These enzymes release a wide range of sugar oligomers into the apoplast, some of which trigger the activation of host immunity via host surface receptors. Recent characterization of cell walls from plant-colonizing fungi have emphasized the abundance of {beta}-glucans in different cell wall layers, which makes them suitable targets for recognition. To characterize host components involved in immunity against fungi, we performed a protein pull-down with the biotinylated {beta}-glucan laminarin. Thereby, we identified a glycoside hydrolase family 81-type glucan-binding protein (GBP) as the major {beta}-glucan interactor. Mutation of GBP1 and its only paralogue GBP2 in barley led to decreased colonization by the beneficial root endophytes Serendipita indica and S. vermifera, as well as the arbuscular mycorrhizal fungus Rhizophagus irregularis. The reduction of symbiotic colonization was accompanied by enhanced responses at the host cell wall. Moreover, GBP mutation in barley also increased resistance to fungal infections in roots and leaves by the hemibiotrophic pathogen Bipolaris sorokiniana and the obligate biotrophic pathogen Blumeria graminis f. sp. hordei, respectively. These results indicate that GBP1 is involved in the establishment of symbiotic associations with beneficial fungi, a role that has potentially been appropriated by barley-adapted pathogens.



O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=134 SRC="FIGDIR/small/536646v1_figu1.gif" ALT="Figure 1">
View larger version (39K):
org.highwire.dtl.DTLVardef@c47957org.highwire.dtl.DTLVardef@fa6727org.highwire.dtl.DTLVardef@18a54d2org.highwire.dtl.DTLVardef@c6b103_HPS_FORMAT_FIGEXP  M_FIG C_FIG In BriefGBP1, a family 81 glycoside hydrolase, is an important {beta}-glucan interactor in barley. Mutation of GBP1 and its sole paralogue GBP2 leads to reduced colonization by beneficial root endophytes, AM fungi and pathogens, accompanied by enhanced responses at the plant cell wall. This indicates that GBP1 and {beta}-glucans are compatibility factors involved in the establishment of symbiotic associations with beneficial fungi, a role possibly hijacked by pathogens.
]]></description>
<dc:creator>Wanke, A.</dc:creator>
<dc:creator>van Boerdonk, S.</dc:creator>
<dc:creator>Mahdi, L. K.</dc:creator>
<dc:creator>Wawra, S.</dc:creator>
<dc:creator>Neidert, M.</dc:creator>
<dc:creator>Chandrasekar, B.</dc:creator>
<dc:creator>Saake, P.</dc:creator>
<dc:creator>Saur, I. M. L.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Holton, N.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Brands, M.</dc:creator>
<dc:creator>Pauly, M.</dc:creator>
<dc:creator>Acosta, I. F.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Zuccaro, A.</dc:creator>
<dc:date>2023-04-13</dc:date>
<dc:identifier>doi:10.1101/2023.04.12.536646</dc:identifier>
<dc:title><![CDATA[A GH81-type β-glucan-binding protein facilitates colonization by mutualistic fungi in barley]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-04-13</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.04.25.538220v1?rss=1">
<title>
<![CDATA[
ATR2Cala2 from Arabidopsis-infecting downy mildew requires 4 TIR-NLR immune receptors for full recognition 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.04.25.538220v1?rss=1"
</link>
<description><![CDATA[
O_LIArabidopsis Col-0 RPP2A and RPP2B confer recognition of Arabidopsis downy mildew (Hyaloperonospora arabidopsidis [Hpa]) isolate Cala2, but the identity of the recognized ATR2Cala2 effector was unknown.
C_LIO_LITo reveal ATR2Cala2, an F2 population was generated from a cross between Hpa-Cala2 and Hpa-Noks1. We identified ATR2Cala2 as a non-canonical RxLR-type effector that carries a signal peptide, a dEER motif, and WY domains but no RxLR motif. Recognition of ATR2Cala2and its effector function were verified by biolistic bombardment, ectopic expression and Hpa infection.
C_LIO_LIATR2Cala2 is recognized in accession Col-0 but not in Ler-0 in which RPP2A and RPP2B are absent. In ATR2Emoy2 and ATR2Noks1 alleles, a frameshift results in an early stop codon. RPP2A and RPP2B are essential for the recognition of ATR2Cala2. Stable and transient expression of ATR2Cala2 under 35S promoter in Arabidopsis and Nicotiana benthamiana enhances disease susceptibility.
C_LIO_LITwo additional Col-0 TIR-NLR (TNL) genes (RPP2C and RPP2D) adjacent to RPP2A and RPP2B are quantitatively required for full resistance to Hpa-Cala2.
C_LIO_LIWe compared RPP2 haplotypes in multiple Arabidopsis accessions and showed that all 4 genes are present in all ATR2Cala2-recognizing accessions.
C_LI
]]></description>
<dc:creator>Kim, D. S.</dc:creator>
<dc:creator>Woods-Tör, A.</dc:creator>
<dc:creator>Cevik, V.</dc:creator>
<dc:creator>Furzer, O. J.</dc:creator>
<dc:creator>Li, Y.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Tör, M.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2023-04-25</dc:date>
<dc:identifier>doi:10.1101/2023.04.25.538220</dc:identifier>
<dc:title><![CDATA[ATR2Cala2 from Arabidopsis-infecting downy mildew requires 4 TIR-NLR immune receptors for full recognition]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-04-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.05.05.539533v1?rss=1">
<title>
<![CDATA[
Pathogen protein modularity enables elaborate mimicry of a host phosphatase 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.05.05.539533v1?rss=1"
</link>
<description><![CDATA[
Pathogens produce diverse effector proteins to manipulate host cellular processes. However, how functional diversity is generated in an effector repertoire is poorly understood. Many effectors in the devastating plant pathogen Phytophthora contain tandem repeats of the "(L)WY" motif, which are structurally conserved but variable in sequences. Here, we discovered a functional module formed by a specific (L)WY-LWY combination in multiple Phytophthora effectors, which efficiently recruit the Serine/Threonine protein phosphatase 2A (PP2A) core enzyme in plant hosts. Crystal structure of an effector-PP2A complex shows that the (L)WY-LWY module enables hijacking of the host PP2A core enzyme to form functional holoenzymes. While sharing the PP2A-interacting module at the amino terminus, these effectors possess divergent C-terminal LWY units and regulate distinct sets of phosphoproteins in the host. Our results highlight the appropriation of an essential host phosphatase through molecular mimicry by pathogens and diversification promoted by protein modularity in an effector repertoire.
]]></description>
<dc:creator>Li, H.</dc:creator>
<dc:creator>Wang, J.</dc:creator>
<dc:creator>Kuan, T.</dc:creator>
<dc:creator>Tang, B.</dc:creator>
<dc:creator>Feng, L.</dc:creator>
<dc:creator>Wang, J.</dc:creator>
<dc:creator>Cheng, Z.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Hulin, M.</dc:creator>
<dc:creator>Li, Y.</dc:creator>
<dc:creator>Zhai, Y.</dc:creator>
<dc:creator>Hou, Y.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Wang, Y.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:date>2023-05-05</dc:date>
<dc:identifier>doi:10.1101/2023.05.05.539533</dc:identifier>
<dc:title><![CDATA[Pathogen protein modularity enables elaborate mimicry of a host phosphatase]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-05-05</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.05.16.540997v1?rss=1">
<title>
<![CDATA[
Cutin-Derived Oligomers Act as Damage-Associated Molecular Patterns in Arabidopsis thaliana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.05.16.540997v1?rss=1"
</link>
<description><![CDATA[
The cuticle constitutes the outermost defensive barrier of most land plants. It comprises a polymeric matrix - cutin, surrounded by soluble waxes. Moreover, the cuticle constitutes the first line of defense against pathogen invasion, while also protecting the plant from many abiotic stresses. Aliphatic monomers in cutin have been suggested to act as immune elicitors in plants. This study analyses the potential of tomato cutin oligomers to act as damage-associated molecular patterns (DAMPs) able to induce a rapid immune response in the model plant Arabidopsis. Cutin oligomeric mixtures led to Ca2+ influx and MAPK activation in Arabidopsis. Comparable responses were measured for cutin, which was also able to induce a reactive oxygen species (ROS) burst. Furthermore, treatment of Arabidopsis with cutin oligomers resulted in a unique transcriptional reprogramming profile, having many archetypal features of pattern-triggered immunity (PTI). Targeted spectroscopic and spectrometric analyses of the cutin oligomers suggest that the elicitors compounds consist mostly of two up to three 10,16-dihydroxyhexadecanoic acid monomers linked together through ester bonds. This study demonstrates that cutin breakdown products can act as DAMPs; a novel class of elicitors deserving further characterization.
]]></description>
<dc:creator>Moreira, C. J.</dc:creator>
<dc:creator>Escorcio, R.</dc:creator>
<dc:creator>Bento, A.</dc:creator>
<dc:creator>Bjornson, M.</dc:creator>
<dc:creator>Tome, A. S.</dc:creator>
<dc:creator>Martins, C.</dc:creator>
<dc:creator>Fanuel, M.</dc:creator>
<dc:creator>Martins, I.</dc:creator>
<dc:creator>Bakan, B.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Silva Pereira, C.</dc:creator>
<dc:date>2023-05-18</dc:date>
<dc:identifier>doi:10.1101/2023.05.16.540997</dc:identifier>
<dc:title><![CDATA[Cutin-Derived Oligomers Act as Damage-Associated Molecular Patterns in Arabidopsis thaliana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-05-18</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.05.31.543011v1?rss=1">
<title>
<![CDATA[
pOPARA: Vectors for Golden Gate assembly of expression constructs containing the araBAD promoter 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.05.31.543011v1?rss=1"
</link>
<description><![CDATA[
Heterologous protein production is often required to investigate the structural, biochemical, and biophysical properties of a protein of interest. Frequently, optimisation of expression conditions is required to obtain soluble protein and maximise yield. Trialling a variety of solubility and purification tags, as well as constructs containing different regulatory elements, is desirable. Golden Gate cloning allows modular assembly of different constructs using Type IIS restriction enzymes. The pOPIN vector suite, which utilises the T7 expression system, has been adapted to be compatible with Golden Gate assembly. Here, we present the pOPARA vectors. Expression from pOPARA vectors is driven by the araBAD promoter (pBAD) and is induced by addition of arabinose to the culture medium. pOPARA allows modular assembly of expression constructs using Golden Gate cloning with the CDS of interest and an optional C-terminal tag. pOPARA1 contains a carbenicillin resistance cassette flanked by restriction sites to allow exchange of the selectable markers. In pOPARA2, the carbenicillin resistance cassette has been exchanged for a spectinomycin resistance cassette. We demonstrate that both vectors can be used to express and produce a control protein.
]]></description>
<dc:creator>Milnes, L.</dc:creator>
<dc:creator>Youles, M.</dc:creator>
<dc:creator>Maidment, J. H.</dc:creator>
<dc:date>2023-06-02</dc:date>
<dc:identifier>doi:10.1101/2023.05.31.543011</dc:identifier>
<dc:title><![CDATA[pOPARA: Vectors for Golden Gate assembly of expression constructs containing the araBAD promoter]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-06-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.06.06.543870v1?rss=1">
<title>
<![CDATA[
Transgenic expression of Arabidopsis ELONGATION FACTOR-TU RECEPTOR (AtEFR) gene in banana enhances resistance to Banana Xanthomonas Wilt disease 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.06.06.543870v1?rss=1"
</link>
<description><![CDATA[
Banana Xanthomonas wilt (BXW) caused by Xanthomonas campestris pv. musacearum (Xcm) is a severe bacterial disease devastating banana production in East and Central Africa, where banana is cultivated as a staple crop. Classical breeding of banana is challenging because the crop is clonally propagated and has limited genetic diversity. Thus, genetic engineering serves as a viable alternative for banana improvement. Several studies have shown that interfamily transfer of the elongation factor Tu receptor gene (AtEFR) from Arabidopsis thaliana to other plant families can increase broad-spectrum resistance against bacterial diseases. In this study, transgenic events of banana cultivar dwarf Cavendish expressing the AtEFR gene were generated and evaluated for resistance against Xcm under greenhouse conditions. The transgenic banana events were responsive to the EF-Tu-derived elf18 peptide and exhibited enhanced resistance to BXW disease compared to non-transgenic control plants. This study suggests that the functionality of AtEFR is retained in banana with the potential of enhancing resistance to BXW disease under field conditions.
]]></description>
<dc:creator>Adero, M.</dc:creator>
<dc:creator>Tripathi, J.</dc:creator>
<dc:creator>Odour, R.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Tripathi, L.</dc:creator>
<dc:date>2023-06-07</dc:date>
<dc:identifier>doi:10.1101/2023.06.06.543870</dc:identifier>
<dc:title><![CDATA[Transgenic expression of Arabidopsis ELONGATION FACTOR-TU RECEPTOR (AtEFR) gene in banana enhances resistance to Banana Xanthomonas Wilt disease]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-06-07</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.08.19.553964v1?rss=1">
<title>
<![CDATA[
The phosphorylation landscape of infection-related development by the rice blast fungus 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.08.19.553964v1?rss=1"
</link>
<description><![CDATA[
Many of the worlds most devastating crop diseases are caused by fungal pathogens which elaborate specialized infection structures to invade plant tissue. Here we present a quantitative mass spectrometry-based phosphoproteomic analysis of infection-related development by the rice blast fungus Magnaporthe oryzae, which threatens global food security. We mapped 8,005 phosphosites on 2,062 fungal proteins, revealing major re-wiring of phosphorylation-based signaling cascades during fungal infection. Comparing phosphosite conservation across 41 fungal species reveals phosphorylation signatures specifically associated with biotrophic and hemibiotrophic fungal infection. We then used parallel reaction monitoring to identify phosphoproteins directly regulated by the Pmk1 MAP kinase that controls plant infection by M. oryzae. We define 33 substrates of Pmk1 and show that Pmk1-dependent phosphorylation of a newly identified regulator, Vts1, is required for rice blast disease. Defining the phosphorylation landscape of infection therefore identifies potential therapeutic interventions for control of plant diseases.
]]></description>
<dc:creator>Cruz-Mireles, N.</dc:creator>
<dc:creator>Oses-Ruiz, M.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Jegousse, C.</dc:creator>
<dc:creator>Ryder, L. S.</dc:creator>
<dc:creator>Bautista, M.-J.</dc:creator>
<dc:creator>Eseola, A. B.</dc:creator>
<dc:creator>Tang, B.</dc:creator>
<dc:creator>Yan, X.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Findlay, K. C.</dc:creator>
<dc:creator>Were, V.</dc:creator>
<dc:creator>MacLean, D.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:date>2023-08-20</dc:date>
<dc:identifier>doi:10.1101/2023.08.19.553964</dc:identifier>
<dc:title><![CDATA[The phosphorylation landscape of infection-related development by the rice blast fungus]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-08-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.08.23.554490v1?rss=1">
<title>
<![CDATA[
Allosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.08.23.554490v1?rss=1"
</link>
<description><![CDATA[
Transmembrane signaling by plant receptor kinases (RKs) has long been thought to involve reciprocal trans-phosphorylation of their intracellular kinase domains. The fact that many of these are pseudokinase domains, however, suggests that additional mechanisms must govern RK signaling activation. Non-catalytic signaling mechanisms of protein kinase domainshave been described in metazoans, but information is scarce for plants. Recently, a non-catalytic function was reported for the leucine-rich repeat (LRR)-RK subfamily XIIa member EFR (ELONGATION FACTOR TU RECEPTOR) and phosphorylation-dependent conformational changes were proposed to regulate signaling of RKs with non-RD kinase domains. Here, using EFR as a model, we describe a non-catalytic activation mechanism for LRR-RKs with non-RD kinase domains. EFR is an active kinase, but a kinase-dead variant retains the ability to enhance catalytic activity of its co-receptor kinase BAK1/SERK3 (BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1/SOMATIC EMBRYOGENESIS RECEPTOR KINASE 3). Applying hydrogen-deuterium exchange mass spectrometry (HDX-MS) analysis and designing homology-based intragenic suppressor mutations, we provide evidence that the EFR kinase domain must adopt its active conformation in order to activate BAK1 allosterically, likely by supporting C-helix positioning in BAK1. Our results suggest a conformational toggle model for signaling, in which BAK1 first phosphorylates EFR in the activation loop to stabilize its active conformation, allowing EFR in turn to allosterically activate BAK1.
]]></description>
<dc:creator>Mühlenbeck, H.</dc:creator>
<dc:creator>Tsutsui, Y.</dc:creator>
<dc:creator>Lemmon, M.</dc:creator>
<dc:creator>Bender, K. W.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2023-08-25</dc:date>
<dc:identifier>doi:10.1101/2023.08.23.554490</dc:identifier>
<dc:title><![CDATA[Allosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-08-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.09.13.557537v1?rss=1">
<title>
<![CDATA[
Genomic analysis of Coccomyxa viridis, a common low-abundance alga associated with lichen symbioses 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.09.13.557537v1?rss=1"
</link>
<description><![CDATA[
Lichen symbiosis is centered around a relationship between a fungus and a photosynthetic microbe, usually a green alga. In addition to their main photosynthetic partner (the photobiont), lichen symbioses can contain additional algae present in low abundance. The biology of these algae and the way they interact with the rest of lichen symbionts remains largely unknown. Here we present the first genome sequence of a non-photobiont lichen-associated alga. Coccomyxa viridis was unexpectedly found in 12% of publicly available lichen metagenomes. With few exceptions, members of the Coccomyxa viridis clade occur in lichens as non-photobionts, potentially growing in thalli endophytically. The 45.7 Mbp genome of C. viridis was assembled into 18 near chromosome-level contigs, making it one of the most contiguous genomic assemblies for any lichen-associated algae. Comparing the C. viridis genome to its close relatives revealed the presence of traits associated with the lichen lifestyle. The genome of C. viridis provides a new resource for exploring the evolution of the lichen symbiosis, and how symbiotic lifestyles shaped evolution in green algae.
]]></description>
<dc:creator>Tagirdzhanova, G.</dc:creator>
<dc:creator>Scharnagl, K.</dc:creator>
<dc:creator>Yan, X.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:date>2023-09-13</dc:date>
<dc:identifier>doi:10.1101/2023.09.13.557537</dc:identifier>
<dc:title><![CDATA[Genomic analysis of Coccomyxa viridis, a common low-abundance alga associated with lichen symbioses]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-09-13</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.10.09.561229v1?rss=1">
<title>
<![CDATA[
Duplication and neofunctionalization of a horizontally-transferred xyloglucanase as a facet of the red queen co-evolutionary dynamic 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.10.09.561229v1?rss=1"
</link>
<description><![CDATA[
Oomycetes are heterotrophic protists that share phenotypic similarities with fungi, including the ability to cause plant diseases, but branch in a separate and distant region of the eukaryotic tree of life. It has been suggested that multiple horizontal gene transfers (HGTs) from fungi-to-oomycetes contributed to the evolution of plant-pathogenic traits. These HGTs are predicted to include secreted proteins that degrade plant cell walls. This is a key trait in the pathology of many oomycetes, as the plant cell wall represents a primary barrier to pathogen invasion and a rich source of carbohydrates. Many of the HGT gene families identified have undergone multiple rounds of duplication. Using a combination of phylogenomic analysis and functional assays, we investigate the diversification of a horizontally-transferred xyloglucanase gene family in the model oomycete species Phytophthora sojae. Our analyses detect 11 genes retained in P. sojae among a complex pattern of gene duplications and losses. Using a phenotype assay, based on heterologous expression in yeast, we show that eight of these paralogs have xyloglucanase function, including variants with distinct protein characteristics, such as a long-disordered C-terminal extension that can increase xyloglucanase activity. The functional xyloglucanase variants analysed subtend an ancestral node close to the fungi-oomycetes gene transfer, suggesting the horizontally-transferred gene was a bona fide xyloglucanase. Expression of xyloglucanase paralogs in Nicotiana benthamiana triggers distinct patterns of reactive oxygen species (ROS) generation, demonstrating that enzyme variants differentially stimulate pattern-triggered immunity in plants. Mass spectrometry of detectable enzymatic products demonstrates that some paralogs catalyze production of variant breakdown profiles, suggesting that secretion of multiple xyloglucanase variants increases efficiency of xyloglucan breakdown, as well as potentially diversifying the range of Damage-Associated Molecular Patterns (DAMPs) released during pathogen attack. We suggest that such patterns of protein neofunctionalization, and variant host responses, represent an aspect of the Red Queen host-pathogen co-evolutionary dynamic.

Significance StatementThe oomycetes are a diverse group of eukaryotic microbes that include some of the most devastating pathogens of plants. Oomycetes perceive, invade, and colonize plants in similar ways to fungi, in part because they acquired the genes to attack and feed on plants from fungi. These genes are predicted to be useful to oomycete plant pathogens because they have undergone multiple rounds of gene duplication. One key enzyme for attacking plant cell wall structures is called xyloglucanase. Xyloglucanase in the oomycetes has undergone multiple rounds of gene duplication, leading to variants including an enzyme with a C-terminal extension that increases activity. Some xyloglucanase variants trigger unique patterns of reactive oxygen species (ROS) in planta, and generate different profiles of cell wall breakdown products - such outcomes could act to mystify and increase the workload of the plant immune system, allowing successful pathogens to proliferate.
]]></description>
<dc:creator>Attah, V.</dc:creator>
<dc:creator>Milner, D. S.</dc:creator>
<dc:creator>Fang, Y.</dc:creator>
<dc:creator>Yan, X.</dc:creator>
<dc:creator>Leonard, G.</dc:creator>
<dc:creator>Heitman, J.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Richards, T. A.</dc:creator>
<dc:date>2023-10-09</dc:date>
<dc:identifier>doi:10.1101/2023.10.09.561229</dc:identifier>
<dc:title><![CDATA[Duplication and neofunctionalization of a horizontally-transferred xyloglucanase as a facet of the red queen co-evolutionary dynamic]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-10-09</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.10.18.562914v1?rss=1">
<title>
<![CDATA[
Zinc-finger (ZiF) fold secreted effectors form a functionally diverse family across lineages of the blast fungus Magnaporthe oryzae. 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.10.18.562914v1?rss=1"
</link>
<description><![CDATA[
Filamentous plant pathogens deliver effector proteins into host cells to suppress host defence responses and manipulate metabolic processes to support colonization. Understanding the evolution and molecular function of these effectors provides knowledge about pathogenesis and can suggest novel strategies to reduce damage caused by pathogens. However, effector proteins are highly variable, share weak sequence similarity and, although they can be grouped according to their structure, only a few structurally conserved effector families have been functionally characterized to date. Here, we demonstrate that Zinc-finger fold (ZiF) secreted proteins form a functionally diverse effector family in the blast fungus Magnaporthe oryzae. This family relies on the Zinc-finger motif for protein stability and is ubiquitously present, forming different effector tribes in blast fungus lineages infecting 13 different host species. Homologs of the canonical ZiF effector, AVR-Pii from rice infecting isolates, are present in multiple M. oryzae lineages, and the wheat infecting strains of the fungus, for example, possess an allele that also binds host Exo70 proteins and activates the immune receptor Pii. Furthermore, ZiF tribes vary in the host Exo70 proteins they bind, indicating functional diversification and an intricate effector/host interactome. Altogether, we uncovered a new effector family with a common protein fold that has functionally diversified in lineages of M. oryzae. This work expands our understanding of the diversity of M. oryzae effectors, the molecular basis of plant pathogenesis and may ultimately facilitate the development of new sources for pathogen resistance.

Author SummaryDiseases caused by filamentous plant pathogens impact global food production, leading to severe economic and humanitarian consequences. These pathogens secrete hundreds of effectors inside the host to alter cellular processes and to promote infection and disease. Effector proteins have weak or no sequence similarity but can be grouped in structural families based on conserved protein folds. However, very few conserved effector families have been functionally characterized. We have identified a family of effectors with a shared Zinc-finger protein fold (ZiF) that is present in lineages of the blast fungus Magnaporthe oryzae that can, collectively, infect 13 different grasses. We characterized the binding of a sub-set of these proteins to putative Exo70 host targets and showed they can be recognized by the plant immune system. Furthermore, we show that other ZiF effectors do not bind Exo70 targets, suggesting functional specialization within this effector family for alternative interactors. These findings shed light on the diversity of effectors and their molecular functions, as well as potentially leading to the development of new sources of blast disease resistance in the future.
]]></description>
<dc:creator>Concepcion, J. C. D. l.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Fujisaki, K.</dc:creator>
<dc:creator>Were, V.</dc:creator>
<dc:creator>Yan, X.</dc:creator>
<dc:creator>Lam, A. H. C.</dc:creator>
<dc:creator>Saado, I.</dc:creator>
<dc:creator>Brabham, H.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Yoshida, K.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2023-10-20</dc:date>
<dc:identifier>doi:10.1101/2023.10.18.562914</dc:identifier>
<dc:title><![CDATA[Zinc-finger (ZiF) fold secreted effectors form a functionally diverse family across lineages of the blast fungus Magnaporthe oryzae.]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-10-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.10.23.563533v1?rss=1">
<title>
<![CDATA[
The NRC0 gene cluster of sensor and helper NLR immune receptors is functionally conserved across asterid plants 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.10.23.563533v1?rss=1"
</link>
<description><![CDATA[
NLR (nucleotide-binding domain and leucine-rich repeat-containing) proteins can form complex receptor networks to confer innate immunity. NRCs are phylogenetically related nodes that function downstream of a massively expanded network of disease resistance proteins that protect against multiple plant pathogens. Here, we used phylogenomic methods to reconstruct the macroevolution of the NRC family. One of the NRCs, we termed NRC0, is the only family member shared across asterid plants, leading us to investigate its evolutionary history and genetic organization. In several asterid species, NRC0 is genetically clustered to other NLRs that are phylogenetically related to NRC-dependent disease resistance genes. This prompted us to hypothesize that the ancestral state of the NRC network is an NLR helper-sensor gene cluster that was present early during asterid evolution. We validated this hypothesis by demonstrating that NRC0 is essential for the hypersensitive cell death induced by its genetically linked sensor NLR partners in four divergent asterid species: tomato, wild sweet potato, coffee and carrot. In addition, activation of a sensor NLR leads to high-order complex formation of its genetically linked NRC0 similar to other NRCs. Our findings map out contrasting evolutionary dynamics in the macroevolution of the NRC network over the last 125 million years from a functionally conserved NLR gene cluster to a massive genetically dispersed network.

One-sentence summaryNRC0 gene cluster is functionally conserved across divergent asterid species and predates the massively expanded NRC network.
]]></description>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Martinez-Anaya, C.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:date>2023-10-23</dc:date>
<dc:identifier>doi:10.1101/2023.10.23.563533</dc:identifier>
<dc:title><![CDATA[The NRC0 gene cluster of sensor and helper NLR immune receptors is functionally conserved across asterid plants]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-10-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.11.27.568785v1?rss=1">
<title>
<![CDATA[
Genetically-clustered antifungal phytocytokines and receptor proteins function together to trigger plant immune signaling 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.11.27.568785v1?rss=1"
</link>
<description><![CDATA[
O_LIPhytocytokines regulate plant immunity via cell-surface receptors. Populus trichocarpa RUST INDUCED SECRETED PEPTIDE 1 (PtRISP1) exhibits an elicitor activity in poplar, as well as a direct antimicrobial activity against rust fungi. PtRISP1 gene directly clusters with a gene encoding a leucine-rich repeat receptor protein (LRR-RP), that we termed RISP- ASSOCIATED LRR-RP (PtRALR).
C_LIO_LIIn this study, we used phylogenomics to characterize the RISP and RALR gene families, and functional assays to characterize RISP/RALR pairs.
C_LIO_LIBoth RISP and RALR gene families specifically evolved in Salicaceae species (poplar and willow), and systematically cluster in the genomes. Two divergent RISPs, PtRISP1 and Salix purpurea RISP1 (SpRISP1), induced a reactive oxygen species (ROS) burst and mitogen- activated protein kinases (MAPKs) phosphorylation in Nicotiana benthamiana leaves expressing the respective clustered RALR. PtRISP1 triggers a rapid stomatal closure in poplar, and both PtRISP1 and SpRISP1 directly inhibit rust pathogen growth.
C_LIO_LIAltogether, these results suggest that plants evolved phytocytokines with direct antimicrobial activities, and that the genes coding these phytocytokines co-evolved and physically cluster with their cognate receptors.
C_LI
]]></description>
<dc:creator>Lintz, J.</dc:creator>
<dc:creator>Goto, Y.</dc:creator>
<dc:creator>Bender, K. W.</dc:creator>
<dc:creator>Bchini, R.</dc:creator>
<dc:creator>Dubrulle, G.</dc:creator>
<dc:creator>Cawston, E.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Duplessis, S.</dc:creator>
<dc:creator>PETRE, B.</dc:creator>
<dc:date>2023-11-27</dc:date>
<dc:identifier>doi:10.1101/2023.11.27.568785</dc:identifier>
<dc:title><![CDATA[Genetically-clustered antifungal phytocytokines and receptor proteins function together to trigger plant immune signaling]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-11-27</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.11.29.569073v1?rss=1">
<title>
<![CDATA[
Subfamily C7 Raf-like kinases MRK1, RAF26, and RAF39 regulate immune homeostasis and stomatal opening in Arabidopsis thaliana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.11.29.569073v1?rss=1"
</link>
<description><![CDATA[
The calcium-dependent protein kinase CPK28 is a regulator of immune homeostasis in multiple plant species. Here, we used a proteomics approach to uncover CPK28-associated proteins. We found that CPK28 associates with subfamily C7 Raf-like kinases MRK1, RAF26, and RAF39, and trans-phosphorylates RAF26 and RAF39. Metazoan Raf kinases function in mitogen-activated protein kinase (MAPK) cascades as MAPK kinase kinases (MKKKs). Although Raf-like kinases share some features with MKKKs, we found that MRK1, RAF26, and RAF39 are unable to trans-phosphorylate any of the 10 Arabidopsis MKKs. We show that MRK1, RAF26, and RAF39 localize to the cytosol and endomembranes, and we define redundant roles for these kinases in stomatal opening, immune-triggered reactive oxygen species (ROS) production, and resistance to a bacterial pathogen. Overall, our study suggests that C7 Raf-like kinases associate with and are phosphorylated by CPK28, function redundantly in stomatal immunity, and possess substrate specificities distinct from canonical MKKKs.
]]></description>
<dc:creator>Dias, M. G.</dc:creator>
<dc:creator>Doss, B.</dc:creator>
<dc:creator>Rawat, A. R.</dc:creator>
<dc:creator>Siegel, K. R.</dc:creator>
<dc:creator>Mahathanthrige, T.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Dharmasena, T.</dc:creator>
<dc:creator>Cameron, E.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Monaghan, J.</dc:creator>
<dc:date>2023-12-01</dc:date>
<dc:identifier>doi:10.1101/2023.11.29.569073</dc:identifier>
<dc:title><![CDATA[Subfamily C7 Raf-like kinases MRK1, RAF26, and RAF39 regulate immune homeostasis and stomatal opening in Arabidopsis thaliana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-12-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.11.30.569466v1?rss=1">
<title>
<![CDATA[
The nucleotide binding domain of NRC-dependent disease resistance proteins is sufficient to activate downstream helper NLR oligomerization and immune signaling 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.11.30.569466v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding domain and leucine-rich repeat (NLR) proteins with pathogen sensor activities have evolved to initiate immune signaling by activating helper NLRs. However, the mechanisms underpinning helper NLR activation by sensor NLRs remain poorly understood. Although coiled-coil (CC) type sensor NLRs such as the Potato virus X disease resistance protein Rx have been shown to activate the oligomerization of their downstream helpers NRC2 and NRC4, the domains involved in sensor-helper signaling are not known. Here, we show that the nucleotide binding (NB) domain within the NB-ARC of the Potato virus X disease resistance protein Rx is necessary and sufficient for oligomerization and immune signaling of downstream helper NLRs. In addition, the NB domains of the disease resistance proteins Gpa2 (cyst nematode resistance), Rpi-amr1, Rpi-amr3 (oomycete resistance) and Sw-5b (virus resistance) are also sufficient to activate their respective downstream NRC helpers. Moreover, the NB domain of Rx and its helper NRC2 form a minimal functional unit that can be transferred from solanaceous plants (lamiids) to the Campanulid species lettuce (Lactuca sativa). Our results challenge the prevailing paradigm that NLR proteins exclusively signal via their N-terminal domains and reveal a signaling activity for the NB domain of NRC-dependent sensor NLRs. We propose a model in which helper NLRs monitor the status of the NB domain of their upstream sensors.
]]></description>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Thompson, R.</dc:creator>
<dc:creator>Claeys, J.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2023-12-01</dc:date>
<dc:identifier>doi:10.1101/2023.11.30.569466</dc:identifier>
<dc:title><![CDATA[The nucleotide binding domain of NRC-dependent disease resistance proteins is sufficient to activate downstream helper NLR oligomerization and immune signaling]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-12-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.12.14.571630v1?rss=1">
<title>
<![CDATA[
A root-specific NLR network confers resistance to plant parasitic nematodes 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.12.14.571630v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding domain and leucine-rich repeat immune receptors (NLRs) confer disease resistance to a multitude of foliar and root parasites of plants. However, the extent to which NLR immunity is expressed differentially between plant organs is poorly known. Here, we show that a large cluster of tomato genes, which encodes the cyst and root-knot nematode disease resistance proteins Hero and MeR1 as well as the NLR-helper NRC6, exhibits nearly exclusive expression in the roots. This root-specific gene cluster emerged in Solanum species about 21 million years ago through gene duplication from the ancient NRC network of asterid plants. NLR-sensors in this gene cluster exclusively signal through NRC6 helpers to trigger the hypersensitive cell death immune response. These findings indicate that the NRC6 gene cluster has sub-functionalized from the larger NRC network to specialize for resistance against root pathogens, including cyst and root-knot nematodes. We propose that NLR gene clusters and networks have evolved organ-specific gene expression as an adaptation to particular parasites and to reduce the risk of autoimmunity.
]]></description>
<dc:creator>Luedke, D.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Posbeyikian, A.</dc:creator>
<dc:creator>Frijters, R.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Ernst, K.</dc:creator>
<dc:creator>Ganal, M.</dc:creator>
<dc:creator>Verhage, A.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2023-12-14</dc:date>
<dc:identifier>doi:10.1101/2023.12.14.571630</dc:identifier>
<dc:title><![CDATA[A root-specific NLR network confers resistance to plant parasitic nematodes]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-12-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.12.17.572070v1?rss=1">
<title>
<![CDATA[
Activation of plant immunity through conversion of a helper NLR homodimer into a resistosome 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.12.17.572070v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding domain and leucine-rich repeat (NLR) proteins can engage in complex interactions to detect pathogens and execute a robust immune response via downstream helper NLRs. However, the biochemical mechanisms of helper NLR activation by upstream sensor NLRs remain poorly understood. Here, we show that the coiled-coil helper NLR NRC2 accumulates in vivo as a homodimer that converts into a higher order oligomer upon activation by its upstream virus disease resistance protein Rx. The Cryo-EM structure of NRC2 in its resting state revealed intermolecular interactions that mediate homodimer formation. These dimerization interfaces have diverged between paralogous NRC proteins to insulate critical network nodes and enable redundant immune pathways. Our results expand the molecular mechanisms of NLR activation pointing to transition from homodimers to higher-order oligomeric resistosomes.
]]></description>
<dc:creator>Selvaraj, M.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Yuen, E. L. H.</dc:creator>
<dc:creator>Ibrahim, T.</dc:creator>
<dc:creator>Zhao, H.</dc:creator>
<dc:creator>Xie, R.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Petre, B.</dc:creator>
<dc:creator>Lawson, D. M.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:date>2023-12-18</dc:date>
<dc:identifier>doi:10.1101/2023.12.17.572070</dc:identifier>
<dc:title><![CDATA[Activation of plant immunity through conversion of a helper NLR homodimer into a resistosome]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-12-18</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.12.12.571219v1?rss=1">
<title>
<![CDATA[
Functional divergence shaped the network architecture of plant immune receptors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.12.12.571219v1?rss=1"
</link>
<description><![CDATA[
In solanaceous plants, several sensor NLRs and their helper NLRs, known as NRC, form a complex network to confer immunity against pathogens. While the sensor NLRs and downstream NRC helpers display diverse genetic compatibility, the evolution and molecular basis of the complex network structure remained elusive. Here we demonstrated that functional divergence of NRC3 variants has shaped the genetic architecture of the NLR network. Natural NRC3 variants form three allelic groups displaying distinct compatibilities with sensor NLRs. Ancestral sequence reconstruction and analyses of natural and chimeric variants identified six key amino acids involved in sensor-helper compatibility, with two residues critical for subfunctionalization. Co-functioning Rpi-blb2 and NRC3 variants showed stronger transient interactions upon effector detection, with NRC3 membrane-associated complexes forming subsequently. Our findings reveal how mutations in helper NLRs, particularly NRC3, have driven the evolution of their transient interactions with sensor NLRs, leading to subfunctionalization and contributing significantly to the complexity of the NRC network in plant immunity.

TeaserHelper NLR subfunctionalization alters transient interactions with sensor NLRs, enhancing plant immune system complexity.
]]></description>
<dc:creator>Huang, C.-Y.</dc:creator>
<dc:creator>Huang, Y.-S.</dc:creator>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:creator>Wang, H.-Y.</dc:creator>
<dc:creator>Huang, L.-T.</dc:creator>
<dc:creator>Lopez-Agudelo, J. C.</dc:creator>
<dc:creator>Chen, Y.-F.</dc:creator>
<dc:creator>Lin, K.-Y.</dc:creator>
<dc:creator>Chiang, B.-J.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:date>2023-12-13</dc:date>
<dc:identifier>doi:10.1101/2023.12.12.571219</dc:identifier>
<dc:title><![CDATA[Functional divergence shaped the network architecture of plant immune receptors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-12-13</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.12.13.571443v1?rss=1">
<title>
<![CDATA[
The leucine-rich repeat receptor kinase QSK1 is a novel regulator of PRR-RBOHD complex and is employed by the bacterial effector HopF2Pto to modulate plant immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.12.13.571443v1?rss=1"
</link>
<description><![CDATA[
Plants detect pathogens using cell-surface pattern recognition receptors (PRRs) like EFR and FLS2, which recognize bacterial EF-Tu and flagellin, respectively. These PRRs, belonging to the leucine-rich repeat receptor kinase (LRR-RK) family, activate the production of reactive oxygen species via the NADPH oxidase RBOHD. The PRR-RBOHD complex is tightly regulated to prevent unwarranted or exaggerated immune responses. However, certain pathogenic effectors can subvert these regulatory mechanisms, thereby suppressing plant immunity. To elucidate the intricate dynamics of the PRR-RBOHD complex, we conducted a comparative co-immunoprecipitation analysis using EFR, FLS2, and RBOHD. We identified QSK1, an LRR-RK, as a novel component of the PRR-RBOHD complex. QSK1 functions as a negative regulator of PRR-triggered immunity (PTI) by downregulating the abundance of FLS2 and EFR. QSK1 is targeted by the bacterial effector HopF2Pto, a mono-ADP ribosyltransferase, resulting in the reduction of FLS2 and EFR levels through both transcriptional and transcription-independent pathways, thereby inhibiting PTI. Furthermore, HopF2Pto reduces transcript levels of PROSCOOP genes encoding important stress-regulated phytocytokines and their receptor MIK2. Importantly, HopF2Pto requires QSK1 for its accumulation and virulence functions within plants. In summary, our results provide novel insights into the mechanism by which HopF2Pto employs QSK1 to desensitize plants to pathogen attack.

One Sentence SummaryQSK1, a novel component in the plant immune receptor complex, downregulates these receptors and phytocytokines, and is exploited by bacterial effector HopF2Pto to desensitize plants to pathogen attack.
]]></description>
<dc:creator>Goto, Y.</dc:creator>
<dc:creator>Kadota, Y.</dc:creator>
<dc:creator>Mbengue, M.</dc:creator>
<dc:creator>Lewis, J. D.</dc:creator>
<dc:creator>Matsui, H.</dc:creator>
<dc:creator>Maki, N.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Shibata, A.</dc:creator>
<dc:creator>Ichihashi, Y.</dc:creator>
<dc:creator>Guttman, D.</dc:creator>
<dc:creator>Nakagami, H.</dc:creator>
<dc:creator>Suzuki, T.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Robatzek, S.</dc:creator>
<dc:creator>Desveaux, D.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Shirasu, K.</dc:creator>
<dc:date>2023-12-14</dc:date>
<dc:identifier>doi:10.1101/2023.12.13.571443</dc:identifier>
<dc:title><![CDATA[The leucine-rich repeat receptor kinase QSK1 is a novel regulator of PRR-RBOHD complex and is employed by the bacterial effector HopF2Pto to modulate plant immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-12-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.01.18.575556v1?rss=1">
<title>
<![CDATA[
Leveraging co-evolutionary insights and AI-based structural modeling to unravel receptor-peptide ligand-binding mechanisms 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.01.18.575556v1?rss=1"
</link>
<description><![CDATA[
Secreted signaling peptides are central regulators of growth, development, and stress responses, but specific steps in the evolution of these peptides and their receptors are not well understood. In addition, the molecular mechanisms of peptide-receptor binding are only known for a few examples, primarily owing to the limited availability of structural capabilities to few laboratories worldwide. Plants have evolved a multitude of secreted signaling peptides and corresponding transmembrane receptors. Stress-responsive SERINE RICH ENDOGENOUS PEPTIDES (SCOOPs) were recently identified. Bioactive SCOOPs are proteolytically processed by subtilases and are perceived by the leucine-rich repeat receptor kinase MALE DISCOVERER 1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) in the model plant Arabidopsis thaliana. How SCOOPs and MIK2 have (co-)evolved, and how SCOOPs bind to MIK2 are however still unknown. Using in silico analysis of 350 plant genomes and subsequent functional testing, we revealed the conservation of MIK2 as SCOOP receptor within the plant order Brassicales. We then leveraged AlphaFold-Multimer and comparative genomics to identify two conserved putative SCOOP-MIK2 binding pockets across Brassicales MIK2 homologues predicted to interact with the  SxS motif of otherwise sequence-divergent SCOOPs. Notably, mutagenesis of both predicted binding pockets compromised SCOOP binding to MIK2, SCOOP-induced complex formation between MIK2 and its co-receptor BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1), and SCOOP-induced reactive oxygen species production; thus, confirming our in silico predictions. Collectively, in addition to revealing the elusive SCOOP-MIK2 binding mechanisms, our analytic pipeline combining phylogenomics, AI-based structural predictions, and experimental biochemical and physiological validation provides a blueprint for the elucidation of peptide ligand-receptor perception mechanisms.

Significance statementThis study presents a rapid and inexpensive alternative to classical structure-based approaches for resolving ligand-receptor binding mechanisms. It relies on a multilayered bioinformatic approach that leverages genomic data across diverse species in combination with AI-based structural modeling to identify true ligand and receptor homologues, and subsequently predict their binding mechanisms. In silico findings were validated by multiple experimental approaches, which investigated the effect of amino acid changes in the proposed binding pockets on ligand-binding, complex formation with a co-receptor essential for downstream signaling, and activation of downstream signaling. Our analysis combining evolutionary insights, in silico modeling and functional validation provides a framework for structure-function analysis of other peptide-receptor pairs, which could be easily implemented by most laboratories.
]]></description>
<dc:creator>Snoeck, S.</dc:creator>
<dc:creator>Lee, H. K.</dc:creator>
<dc:creator>Schmid, M. W.</dc:creator>
<dc:creator>Bender, K. W.</dc:creator>
<dc:creator>Neeracher, M. J.</dc:creator>
<dc:creator>Fernandez-Fernandez, A. D.</dc:creator>
<dc:creator>Santiago, J.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2024-01-18</dc:date>
<dc:identifier>doi:10.1101/2024.01.18.575556</dc:identifier>
<dc:title><![CDATA[Leveraging co-evolutionary insights and AI-based structural modeling to unravel receptor-peptide ligand-binding mechanisms]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-01-18</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.01.18.576090v1?rss=1">
<title>
<![CDATA[
Speedy benthi: Elongated photoperiods reduce the generation time of the model plant species Nicotiana benthamiana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.01.18.576090v1?rss=1"
</link>
<description><![CDATA[
Nicotiana benthamiana is increasingly gaining prominence as a model plant species with recently published high-quality genome assemblies, which will further enable forward and reverse genetic approaches (Bally et al., 2018; Derevnina et al., 2019; Kourelis et al., 2019; Ranawaka et al., 2023; Vollheyde et al., 2023). However, the generation time of N. benthamiana poses a bottleneck in the creation of mutant and transgenic plant lines. Speed breeding (SB), by extended photoperiods and adjustments to growth parameters, is an efficient way to reduce generation times for many crop and model plant species (Ghosh et al., 2018; Watson et al., 2018; Hickey et al., 2019; Varshney et al., 2021). We hypothesized that an extended photoperiod could reduce the seed to seed generation time of N. benthamiana. We tested this hypothesis by comparing generation times under SB conditions to traditionally used photoperiods in growth chambers and green house settings. We found that a 22h photoperiod reduced the generation time of N. benthamiana by approximately 2 weeks (16-22%). Fertilization in combination with a far-red light spectrum did not yield a further reduction in generation time when combined with SB conditions. Our findings further contribute to the establishment of N. benthamiana as an important model organism for plant research.
]]></description>
<dc:creator>Castle, M.</dc:creator>
<dc:creator>Luedke, D.</dc:creator>
<dc:date>2024-01-22</dc:date>
<dc:identifier>doi:10.1101/2024.01.18.576090</dc:identifier>
<dc:title><![CDATA[Speedy benthi: Elongated photoperiods reduce the generation time of the model plant species Nicotiana benthamiana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-01-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.01.20.576406v1?rss=1">
<title>
<![CDATA[
The blast effector Pwl2 is a virulence factor that modifies the cellular localisation of host protein HIPP43 to suppress immunity. 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.01.20.576406v1?rss=1"
</link>
<description><![CDATA[
The rice blast fungus Magnaporthe oryzae secretes a battery of effector proteins to facilitate host infection. Among these effectors, Pwl2 was first identified as a host specificity determinant for infection of weeping lovegrass (Eragrostis curvula) and is also recognised by the barley Mla3 resistance gene. However, its biological activity is not known. Here we show that PWL2 expression is regulated by the Pmk1 MAP kinase during cell-to-cell movement by M. oryzae at plasmodesmata (PD)-containing pit field sites. Consistent with its regulation, we provide evidence that Pwl2 binds to a barley heavy metal-binding isoprenylated protein HIPP43, which results in its displacement from plasmodesmata. Transgenic barley lines overexpressing either PWL2 or HIPP43 exhibit attenuated immune responses and increased disease susceptibility. By contrast, a Pwl2SNDEYWY mutant that does not interact with HIPP43, fails to alter the PD localisation of HIPP43. Targeted deletion of three copies of PWL2 in M. oryzae results in a{Delta} pwl2 mutant showing gain-of-virulence to weeping lovegrass and barley Mla3 lines, but also a reduction in severity of blast disease on susceptible host plants. Taken together, our results provide evidence that Pwl2 is a virulence factor that acts by suppressing host immunity through perturbing the plasmodesmatal deployment of HIPP43.
]]></description>
<dc:creator>Were, V.</dc:creator>
<dc:creator>Yan, X.</dc:creator>
<dc:creator>Foster, A.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Bentham, A.</dc:creator>
<dc:creator>Zdrzałek, R.</dc:creator>
<dc:creator>Ryder, L.</dc:creator>
<dc:creator>Kaimenyi, D.</dc:creator>
<dc:creator>Gomez De La Cruz, D.</dc:creator>
<dc:creator>Gentle, A.</dc:creator>
<dc:creator>Petit-Houdenot, Y.</dc:creator>
<dc:creator>Eseola, A. B.</dc:creator>
<dc:creator>Smoker, M.</dc:creator>
<dc:creator>Bautista, M. J.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Maclean, D.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:date>2024-01-23</dc:date>
<dc:identifier>doi:10.1101/2024.01.20.576406</dc:identifier>
<dc:title><![CDATA[The blast effector Pwl2 is a virulence factor that modifies the cellular localisation of host protein HIPP43 to suppress immunity.]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-01-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.02.14.580413v1?rss=1">
<title>
<![CDATA[
Bioengineering secreted proteases converts divergent Rcr3 orthologs and paralogs into extracellular immune co-receptors 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.02.14.580413v1?rss=1"
</link>
<description><![CDATA[
Secreted immune proteases Rcr3 and Pip1 of tomato are both inhibited by Avr2 from the fungal plant pathogen Cladosporium fulvum but only Rcr3 act as a decoy co-receptor that detects Avr2 in the presence of the Cf-2 immune receptor. Here, we identified crucial residues from tomato Rcr3 required for Cf-2-mediated signalling and bioengineered various proteases to trigger Avr2/Cf-2 dependent immunity. Despite substantial divergences in Rcr3 orthologs from eggplant and tobacco, only minimal alterations were sufficient to trigger Avr2/Cf-2-triggered immune signalling. Tomato Pip1, by contrast, was bioengineered with 16 Rcr3-specific residues to initiate Avr2/Cf-2-triggered immune signalling. These residues cluster on one side next to the substrate binding groove, indicating a potential Cf-2 interaction site. Our findings also revealed that Rcr3 and Pip1 have distinct substrate preferences determined by two variant residues and that both are suboptimal for binding Avr2. This study advances our understanding of Avr2 perception and opens avenues to bioengineer proteases to broaden pathogen recognition in other crops.
]]></description>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Schuster, M.</dc:creator>
<dc:creator>Demir, F.</dc:creator>
<dc:creator>Mattinson, O.</dc:creator>
<dc:creator>Krauter, S.</dc:creator>
<dc:creator>Kahlon, P. S.</dc:creator>
<dc:creator>O'Grady, R.</dc:creator>
<dc:creator>Royston, S.</dc:creator>
<dc:creator>Bravo-Cazar, A. L.</dc:creator>
<dc:creator>Mooney, B. C.</dc:creator>
<dc:creator>Huesgen, P. F.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>van der Hoorn, R. A. L.</dc:creator>
<dc:date>2024-02-15</dc:date>
<dc:identifier>doi:10.1101/2024.02.14.580413</dc:identifier>
<dc:title><![CDATA[Bioengineering secreted proteases converts divergent Rcr3 orthologs and paralogs into extracellular immune co-receptors]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-02-15</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.02.13.580079v1?rss=1">
<title>
<![CDATA[
Multiple horizontal mini-chromosome transfers drive genome evolution of clonal blast fungus lineages 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.02.13.580079v1?rss=1"
</link>
<description><![CDATA[
Crop disease pandemics are often driven by clonal lineages of plant pathogens that reproduce asexually. How these clonal pathogens continuously adapt to their hosts despite harboring limited genetic variation, and in absence of sexual recombination remains elusive. Here, we reveal multiple instances of horizontal chromosome transfer within pandemic clonal lineages of the blast fungus Magnaporthe (Syn. Pyricularia) oryzae. We identified a horizontally transferred 1.2Mb supernumerary mini-chromosome which is remarkably conserved between M. oryzae isolates from both the rice blast fungus lineage and the lineage infecting Indian goosegrass (Eleusine indica), a wild grass that often grows in the proximity of cultivated cereal crops. Furthermore, we show that this mini-chromosome was horizontally acquired by clonal rice blast isolates through at least nine distinct transfer events over the past three centuries. These findings establish horizontal mini-chromosome transfer as a mechanism facilitating genetic exchange among different host-associated blast fungus lineages. We propose that blast fungus populations infecting wild grasses act as genetic reservoirs that drive genome evolution of pandemic clonal lineages that afflict cereal crops.
]]></description>
<dc:creator>Barragan, A. C.</dc:creator>
<dc:creator>Latorre, S. M.</dc:creator>
<dc:creator>Malmgren, A.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Win, J.</dc:creator>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:creator>Burbano, H. A.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:date>2024-02-15</dc:date>
<dc:identifier>doi:10.1101/2024.02.13.580079</dc:identifier>
<dc:title><![CDATA[Multiple horizontal mini-chromosome transfers drive genome evolution of clonal blast fungus lineages]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-02-15</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.03.28.587199v1?rss=1">
<title>
<![CDATA[
A RALF-Brassinosteroid morpho-signaling circuit regulates Arabidopsis hypocotyl cell shape 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.03.28.587199v1?rss=1"
</link>
<description><![CDATA[
Plant cells survey and modulate their cell wall to control their shape and anisotropic growth. Signaling mediated by the plant steroid hormones brassinosteroids (BR) plays a central role in coordinating cell wall status and cell growth, and alterations in the cell wall - BR feedback loop leads to life-threatening defects in tissue and cellular integrity. How the status of the cell wall is relayed to BR signaling remains largely unclear. Increasing evidence shows that RAPID ALKALANIZATION FACTORs (RALFs), a class of secreted peptides, play structural and signaling roles at the cell surface. Here we show that perception of RALF23 promotes the formation and signaling of the main BR receptor complex formed by BRASSINOSTEROID INSENSITIVE 1 (BRI1) and BRI1-BRASSINOSTEROID INSENSITIVE1-BRASSINOSTEROID-ASSOCIATED KINASE 1

(BAK1). The loss of the plasma membrane-localized RALF receptor complex FERONIA (FER)-LORELEI LIKE GPI-anchor protein 1 (LLG1) leads to defects in cell expansion and anisotropy, as well as uncontrolled BRI1-BAK1 complex formation and signaling. RALF23 bioactivity relies on pectin status and its perception induces changes in pectin composition and the activity of pectin-modifying enzymes. Our observations suggest a model in which RALF23 functions as a cell wall-informed signaling cue initiating a feedback loop that solicits BR signaling, modifies the cell wall, and coordinates cell morphogenesis.

Highlights-The RALF receptor complex FER-LLG1 regulates cell anisotropic growth

-RALF23 promotes BRI1-BAK1 complex formation and signaling

-RALF23 functions as a cell wall-informed and wall-modifying signaling cue
]]></description>
<dc:creator>Biermann, D.</dc:creator>
<dc:creator>von Arx, M.</dc:creator>
<dc:creator>Xhelilaj, K.</dc:creator>
<dc:creator>Sere, D.</dc:creator>
<dc:creator>Stegmann, M.</dc:creator>
<dc:creator>Wolf, S.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Gronnier, J.</dc:creator>
<dc:date>2024-03-30</dc:date>
<dc:identifier>doi:10.1101/2024.03.28.587199</dc:identifier>
<dc:title><![CDATA[A RALF-Brassinosteroid morpho-signaling circuit regulates Arabidopsis hypocotyl cell shape]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-03-30</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.01.11.575225v1?rss=1">
<title>
<![CDATA[
An oomycete effector co-opts a host RabGAP protein to remodel pathogen interface and subvert defense-related secretion 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.01.11.575225v1?rss=1"
</link>
<description><![CDATA[
Pathogens have evolved sophisticated mechanisms to manipulate host cell membrane dynamics, a crucial adaptation to survive in hostile environments shaped by innate immune responses. Plant- derived membrane interfaces, engulfing invasive hyphal projections of fungal and oomycete pathogens, are prominent junctures dictating infection outcomes. Understanding how pathogens transform these host-pathogen interfaces to their advantage remains a key biological question. Here, we identified a conserved effector, secreted by plant pathogenic oomycetes, that co-opts a host Rab GTPase-activating protein (RabGAP), TBC1D15L, to remodel the host-pathogen interface. The effector, PiE354, hijacks TBC1D15L as a susceptibility factor to usurp its GAP activity on Rab8a--a key Rab GTPase crucial for defense-related secretion. By hijacking TBC1D15L, PiE354 purges Rab8a from the plasma membrane, diverting Rab8a-mediated immune trafficking away from the pathogen interface. This mechanism signifies an uncanny evolutionary adaptation of a pathogen effector in co- opting a host regulatory component to subvert defense-related secretion, thereby providing unprecedented mechanistic insights into the reprogramming of host membrane dynamics by pathogens.
]]></description>
<dc:creator>Yuen, E. L. H.</dc:creator>
<dc:creator>Tumtas, Y.</dc:creator>
<dc:creator>Chan, L. I.</dc:creator>
<dc:creator>Ibrahim, T.</dc:creator>
<dc:creator>Evangelisti, E.</dc:creator>
<dc:creator>Tulin, F.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Bubeck, D.</dc:creator>
<dc:creator>Schornack, S.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:date>2024-01-15</dc:date>
<dc:identifier>doi:10.1101/2024.01.11.575225</dc:identifier>
<dc:title><![CDATA[An oomycete effector co-opts a host RabGAP protein to remodel pathogen interface and subvert defense-related secretion]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-01-15</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.04.15.589471v1?rss=1">
<title>
<![CDATA[
Arabidopsis WALL-ASSOCIATED KINASES are not required for oligogalacturonide-induced signaling and immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.04.15.589471v1?rss=1"
</link>
<description><![CDATA[
Carbohydrate-based cell wall signaling impacts plant growth, development, and stress responses; however, how cell wall signals are perceived and transduced remains poorly understood. Several cell wall breakdown products have been described as typical damage-associated molecular patterns (DAMPs) that activate plant immunity, including pectin-derived oligogalacturonides (OGs). Receptor kinases (RKs) of the WALL-ASSOCIATED KINASE (WAK) family have been shown to bind pectin and OGs, and were previously proposed as OG receptors. However, unambiguous genetic evidence for the role of WAKs in OG responses is lacking. Here, we investigated the role of Arabidopsis WAKs in OG perception using a novel deletion mutant of the clustered WAK family. Using a combination of immune assays for early and late pattern-triggered immunity (PTI), we show that WAKs are dispensable for OG-induced signaling and immunity, indicating that they are not bona fide OG receptors.
]]></description>
<dc:creator>Herold, L.</dc:creator>
<dc:creator>Hua, C.</dc:creator>
<dc:creator>Kohorn, B.</dc:creator>
<dc:creator>Nuernberger, T.</dc:creator>
<dc:creator>DeFalco, T. A.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2024-04-17</dc:date>
<dc:identifier>doi:10.1101/2024.04.15.589471</dc:identifier>
<dc:title><![CDATA[Arabidopsis WALL-ASSOCIATED KINASES are not required for oligogalacturonide-induced signaling and immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-04-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2023.07.04.547613v1?rss=1">
<title>
<![CDATA[
Mechanosensing and Sphingolipid-Docking Mediate Lipopetide-Induced Immunity in Arabidopsis 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2023.07.04.547613v1?rss=1"
</link>
<description><![CDATA[
Bacteria-derived lipopeptides are immunogenic triggers of host defenses in metazoans and plants. Root-associated rhizobacteria produce cyclic lipopeptides that activate systemically induced resistance (IR) against microbial infection in various plants. How these molecules are perceived by plant cells remains elusive. Here, we reveal that immunity activation in Arabidopsis thaliana by the lipopeptide elicitor surfactin is mediated by docking into specific sphingolipid-enriched domains and relies on host membrane deformation and subsequent activation of mechanosensitive ion channels. This mechanism leads to host defense potentiation and resistance to the necrotroph B. cinerea but is distinct from host pattern recognition receptor-mediated immune activation and reminiscent of damage-induced plant immunity.
]]></description>
<dc:creator>Prsic, J.</dc:creator>
<dc:creator>Gilliard, G.</dc:creator>
<dc:creator>Ibrahim, H.</dc:creator>
<dc:creator>Arguelles Arias, A.</dc:creator>
<dc:creator>Rondelli, V.</dc:creator>
<dc:creator>Crowet, J.-M.</dc:creator>
<dc:creator>Genva, M.</dc:creator>
<dc:creator>Luzuriaga Loaiza, W. P.</dc:creator>
<dc:creator>Deboever, E.</dc:creator>
<dc:creator>Nasir, N.</dc:creator>
<dc:creator>Lins, L.</dc:creator>
<dc:creator>Mathelie-Guinlet, M.</dc:creator>
<dc:creator>Eschrig, S.</dc:creator>
<dc:creator>Ranf, S.</dc:creator>
<dc:creator>Dorey, S.</dc:creator>
<dc:creator>De Coninck, B.</dc:creator>
<dc:creator>Nurnberger, T.</dc:creator>
<dc:creator>Mongrand, S.</dc:creator>
<dc:creator>Hofte, M.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Dufrene, Y.</dc:creator>
<dc:creator>Deleu, M.</dc:creator>
<dc:creator>Ongena, M.</dc:creator>
<dc:date>2023-07-04</dc:date>
<dc:identifier>doi:10.1101/2023.07.04.547613</dc:identifier>
<dc:title><![CDATA[Mechanosensing and Sphingolipid-Docking Mediate Lipopetide-Induced Immunity in Arabidopsis]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2023-07-04</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.01.20.576400v1?rss=1">
<title>
<![CDATA[
Bioengineering a plant NLR immune receptor with a robust binding interface towards a conserved fungal pathogen effector 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.01.20.576400v1?rss=1"
</link>
<description><![CDATA[
Bioengineering of plant immune receptors has emerged as a key strategy for generating novel disease resistance traits to counteract the expanding threat of plant pathogens to global food security. However, current approaches are limited by rapid evolution of plant pathogens in the field and may lack durability when deployed. Here, we show that the rice nucleotide-binding, leucine-rich repeat (NLR) immune receptor Pik-1 can be engineered to respond to a conserved family of effectors from the multihost blast fungus pathogen Magnaporthe oryzae. We switched the effector binding and response profile of the Pik NLR from its cognate rice blast effector AVR-Pik to the host-determining factor Pwl2 by installing a putative host target, OsHIPP43, in place of the native integrated HMA domain (generating Pikm-1OsHIPP43). This chimeric receptor also responded to other PWL alleles from diverse blast isolates. The crystal structure of the Pwl2/OsHIPP43 complex revealed a multifaceted, robust interface that cannot be easily disrupted by mutagenesis, and may therefore provide durable, broad resistance to blast isolates carrying PWL effectors in the field. Our findings highlight how the host targets of pathogen effectors can be used to bioengineer new recognition specificities that have more robust properties compared to naturally evolved disease resistance genes.
]]></description>
<dc:creator>Zdrzalek, R.</dc:creator>
<dc:creator>Xi, Y.</dc:creator>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Bentham, A. R.</dc:creator>
<dc:creator>Petit-Houdenot, Y.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Shimizu, M.</dc:creator>
<dc:creator>Were, V.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Terauchi, R. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2024-01-23</dc:date>
<dc:identifier>doi:10.1101/2024.01.20.576400</dc:identifier>
<dc:title><![CDATA[Bioengineering a plant NLR immune receptor with a robust binding interface towards a conserved fungal pathogen effector]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-01-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.06.16.598756v1?rss=1">
<title>
<![CDATA[
Helper NLR immune protein NRC3 evolved to evade inhibition by a cyst nematode virulence effector 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.06.16.598756v1?rss=1"
</link>
<description><![CDATA[
Parasites can counteract host immunity by suppressing nucleotide binding and leucine-rich repeat (NLR) proteins that function as immune receptors. We previously showed that a cyst nematode virulence effector SPRYSEC15 (SS15) binds and inhibits oligomerisation of helper NLR proteins in the expanded NRC1/2/3 clade by preventing intramolecular rearrangements required for NRC oligomerisation into an activated resistosome. Here we examined the degree to which NRC proteins from multiple Solanaceae species are sensitive to suppression by SS15 and tested hypotheses about adaptive evolution of the binding interface between the SS15 inhibitor and NRC proteins. Whereas all tested orthologs of NRC2 were inhibited by SS15, some natural variants of NRC1 and NRC3 are insensitive to SS15 suppression. Ancestral sequence reconstruction combined with functional assays revealed that NRC3 transitioned from an ancestral suppressed form to an insensitive one over 19 million years ago. Our analyses revealed the evolutionary trajectory of coevolution between a parasite inhibitor and its NLR immune receptor target, identifying key evolutionary transitions in helper NLRs that counteract this inhibition. This work reveals a distinct type of gene-for-gene interaction between parasite or pathogen immunosuppressors and host immune receptors that contrasts with the coevolution between AVR effectors and immune receptors.
]]></description>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Selvaraj, M.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Martinez-Anaya, C.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2024-06-16</dc:date>
<dc:identifier>doi:10.1101/2024.06.16.598756</dc:identifier>
<dc:title><![CDATA[Helper NLR immune protein NRC3 evolved to evade inhibition by a cyst nematode virulence effector]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-06-16</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.06.18.599586v1?rss=1">
<title>
<![CDATA[
A disease resistance protein triggers oligomerization of its NLR helper into a hexameric resistosome to mediate innate immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.06.18.599586v1?rss=1"
</link>
<description><![CDATA[
NRCs are essential helper NLR (nucleotide-binding domain and leucine-rich repeat) proteins that execute the immune response triggered by disease resistance proteins, also known as sensor NLRs. The structure of the resting state of NbNRC2 was recently revealed to be a homodimer. However, the sensor-activated state has not yet been elucidated. In this study, we used cryo-EM to determine the structure of sensor-activated NbNRC2, which forms a hexameric inflammasome-like structure known as resistosome. To confirm the functional significance of the hexamer, we mutagenized the interfaces involved in oligomerization and found that mutations in three nucleotide-binding domain interface residues abolish oligomerization and immune signalling. Comparative structural analyses between the resting state NbNRC2 homodimer and the sensor-activated homohexamer revealed significant structural rearrangements before and after activation, providing insights into NLR activation mechanisms. Furthermore, structural comparisons between the NbNRC2 hexamer and previously reported CC-NLR pentameric assemblies revealed features in NbNRC2 that allow for the integration of an additional protomer. We also used the NbNRC2 hexamer structure to assess the recently released AlphaFold 3 for the prediction of activated CC-NLR oligomers. This revealed that AlphaFold 3 allows for high-confidence modelling of the N-terminal 1-helices of NbNRC2 and other CC-NLRs, a region that has proven difficult to fully resolve using structural approaches. Overall, our work sheds light on the structural and biochemical mechanisms underpinning NLR activation and expands our understanding of NLR structural diversity.
]]></description>
<dc:creator>Madhuprakash, J.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Posbeyikian, A.</dc:creator>
<dc:creator>Richardson, J.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Webster, M. W.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2024-06-19</dc:date>
<dc:identifier>doi:10.1101/2024.06.18.599586</dc:identifier>
<dc:title><![CDATA[A disease resistance protein triggers oligomerization of its NLR helper into a hexameric resistosome to mediate innate immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-06-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.02.01.578334v1?rss=1">
<title>
<![CDATA[
Modular mechanisms of immune priming and growth inhibition mediated by plant effector-triggered immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.02.01.578334v1?rss=1"
</link>
<description><![CDATA[
Excessive activation of effector-triggered immunity (ETI) in plants inhibits plant growth and activates cell death. ETI mediated by intracellular Toll/Interleukin-1 receptor/Resistance protein (TIR) nucleotide-binding leucine-rich-repeat receptors (NLRs) involves two partially redundant signalling nodes in Arabidopsis, EDS1-PAD4-ADR1 and EDS1-SAG101-NRG1. Genetic and transcriptomic analyses show that EDS1-PAD4-ADR1 primarily enhances the immune component abundance and is critical for limiting pathogen growth, whereas EDS1-SAG101-NRG1 mainly activates the hypersensitive cell death response (HR) but is dispensable for immune priming. This study enhances our understanding of the distinct contributions of these two signalling modules to ETI and suggests potential strategies for improving disease resistance in crops without compromising yield.
]]></description>
<dc:creator>Chhillar, H.</dc:creator>
<dc:creator>Yeh, P.-M.</dc:creator>
<dc:creator>Nguyen, H. H.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Ding, P.</dc:creator>
<dc:date>2024-02-01</dc:date>
<dc:identifier>doi:10.1101/2024.02.01.578334</dc:identifier>
<dc:title><![CDATA[Modular mechanisms of immune priming and growth inhibition mediated by plant effector-triggered immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-02-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.06.25.599845v1?rss=1">
<title>
<![CDATA[
Discovery of functional NLRs using expression level, high-throughput transformation, and large-scale phenotyping 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.06.25.599845v1?rss=1"
</link>
<description><![CDATA[
Protecting crops from pests and diseases is vital for the sustainable agricultural systems needed for food security. Introducing functional resistance genes to enhance the plant immune system is an effective method of disease control, but identifying new immune receptors is time-consuming and resource intensive. We observed that functional immune receptors of the NLR class show a signature of high expression in uninfected plants across both monocot and dicot species. Here we show that this signature, combined with high throughput crop transformation, can be used to rapidly identify candidate NLRs from diverse plant species and validate pathogen resistance directly in crop plants. As a proof of concept, we generated a wheat transgenic library carrying 995 NLRs from 18 grass species. Screening the collection with the stem rust pathogen Puccinia graminis, which is a major threat to wheat production, we confirm 19 new resistance genes. This pipeline facilitates resistance gene discovery, unlocking a large gene pool of diverse and non-domesticated plant species and providing in-planta gene validation of disease resistance directly in crops.
]]></description>
<dc:creator>Brabham, H. J.</dc:creator>
<dc:creator>Hernandez-Pinzon, I.</dc:creator>
<dc:creator>Yanagihara, C.</dc:creator>
<dc:creator>Ishikawa, N.</dc:creator>
<dc:creator>Komori, T.</dc:creator>
<dc:creator>Matny, O. N.</dc:creator>
<dc:creator>Hubbard, A.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Feist, A.</dc:creator>
<dc:creator>Numazawa, H.</dc:creator>
<dc:creator>Green, P.</dc:creator>
<dc:creator>Dreiseitl, A.</dc:creator>
<dc:creator>Takemori, N.</dc:creator>
<dc:creator>Komari, T.</dc:creator>
<dc:creator>Freedman, R. P.</dc:creator>
<dc:creator>Steffenson, B.</dc:creator>
<dc:creator>van Esse, H. P.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:date>2024-06-28</dc:date>
<dc:identifier>doi:10.1101/2024.06.25.599845</dc:identifier>
<dc:title><![CDATA[Discovery of functional NLRs using expression level, high-throughput transformation, and large-scale phenotyping]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-06-28</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.07.01.599856v1?rss=1">
<title>
<![CDATA[
Reversible ubiquitination of integrated domain controls paired NLR immune receptor complex homeostasis 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.07.01.599856v1?rss=1"
</link>
<description><![CDATA[
AbstractPlant intracellular NLR immune receptors can function individually or in pairs to detect pathogen effectors and activate immune responses. NLR homeostasis has to be tightly regulated to ensure proper defense without triggering autoimmunity. However, in contrast to singleton NLRs, the mechanisms controlling the paired NLRs complex homeostasis are less understood. The paired Arabidopsis RRS1/RPS4 immune receptor complex confers disease resistance through effector recognition mediated by the integrated WRKY domain of RRS1. Here, through proximity labelling, we reveal a ubiquitination-deubiquitination cycle that controls the homeostasis of the RRS1/RPS4 complex. E3 ligase RARE directly binds and ubiquitinates RRS1s WRKY domain to promote its proteasomal degradation, thereby destabilizing RPS4 indirectly and compromising the stability and function of the RRS1/RPS4 complex. Conversely, the deubiquitinating enzymes UBP12/UBP13 deubiquitinate RRS1s WRKY domain, counteracting RAREs effects. Interestingly, the abundance of WRKY transcription factors WRKY70 and WRKY41 is also regulated by RARE and UBP12/UBP13. Phylogenetic analysis suggests this regulation likely transferred from WRKY70/WRKY41 to RRS1 upon WRKY domain integration. Our findings improve our understanding of homeostatic regulation of paired NLR complex and uncover a new paradigm whereby domain integration can co-opt preexisting post-translational modification to regulate novel protein functions.
]]></description>
<dc:creator>Chen, Z.</dc:creator>
<dc:creator>Huang, J.-h.</dc:creator>
<dc:creator>Li, J.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Guo, H.</dc:creator>
<dc:date>2024-07-03</dc:date>
<dc:identifier>doi:10.1101/2024.07.01.599856</dc:identifier>
<dc:title><![CDATA[Reversible ubiquitination of integrated domain controls paired NLR immune receptor complex homeostasis]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-07-03</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.07.26.605320v1?rss=1">
<title>
<![CDATA[
Molecular mimicry of a pathogen virulence target by a plant immune receptor 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.07.26.605320v1?rss=1"
</link>
<description><![CDATA[
Plants and animals respond to pathogen attack by mounting innate immune responses that require intracellular nucleotide binding leucine-rich repeat (NLR) proteins. These immune receptors detect pathogen infection by sensing virulence effector proteins. However, the mechanisms by which receptors evolve new recognition specificities remain poorly understood. Here we report that a plant NLR has evolved the capacity to bind to a pathogen effector by acting as a molecular mimic of a virulence target of the effector, thereby triggering an immune response. The barley NLR Mildew Locus A 3 (MLA3) confers resistance to the blast fungus Magnaporthe oryzae by recognizing the effector Pwl2. Using structural analysis, we show that MLA3 has acquired the capacity to bind and respond to Pwl2 through molecular mimicry of the effector host target HIPP43. We demonstrate that the amino acids at the binding interface of MLA3 and Pwl2 are highly conserved in interface of HIPP43 with Pwl2, and are required to trigger an immune response. We used this discovery to bioengineer SR50--an MLA ortholog in rye that confers resistance to wheat stem rust--by introducing the Pwl2 binding interface of MLA3. This chimeric receptor has dual recognition activities, binding and responding to effectors from two major cereal pathogens. Collectively, these results provide evidence that plant immune receptors have evolved sophisticated mimicry strategies to counteract pathogen attack.
]]></description>
<dc:creator>Gomez De La Cruz, D.</dc:creator>
<dc:creator>Zdrzałek, R.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:date>2024-07-26</dc:date>
<dc:identifier>doi:10.1101/2024.07.26.605320</dc:identifier>
<dc:title><![CDATA[Molecular mimicry of a pathogen virulence target by a plant immune receptor]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-07-26</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.09.02.610751v1?rss=1">
<title>
<![CDATA[
Transcriptomic profiling of Candidatus Liberibacter asiaticus in different citrus tissues reveals novel insights into Huanglongbing pathogenesis 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.09.02.610751v1?rss=1"
</link>
<description><![CDATA[
Candidatus Liberibacter asiaticus (Las) is a gram-negative bacterial pathogen associated with citrus huanglongbing (HLB) or greening disease. Las is transmitted by the Asian citrus psyllid (ACP) where it colonizes the phloem tissue, resulting in substantial economic losses to citrus industry worldwide. Despite extensive efforts, effective management strategies against HLB remain elusive, necessitating a deeper understanding of the pathogen s biology. Las undergoes cell-to-cell movement through phloem flow and colonizes different tissues in which Las may have varying interactions with the host. Here, we investigate the transcriptomic landscape of Las in citrus seed coat vasculatures, enabling a complete gene expression profiling of Las genome and revealing unique transcriptomic patterns compared to previous studies using midrib tissues. Comparative transcriptomics between seed coat, midrib and ACP identified specific responses and metabolic states of Las in different host tissue. Two Las virulence factors that exhibit higher expression in seed coat can suppress callose deposition. Therefore, they may contribute to unclogging sieve plate pores during Las colonization in seed coat vasculature. Furthermore, analysis of regulatory elements uncovers a potential role of LuxR-type transcription factors in regulating Liberibacter effector gene expression during plant colonization. Together, this work provides novel insights into the pathogenesis of the devastating citrus HLB.

FundingThis work is supported by USDA National Institute of Food and Agriculture award No. 2020-70029-33197 to W.M and A.L.
]]></description>
<dc:creator>Lovelace, A. H.</dc:creator>
<dc:creator>Wang, C.</dc:creator>
<dc:creator>Levy, A.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:date>2024-09-02</dc:date>
<dc:identifier>doi:10.1101/2024.09.02.610751</dc:identifier>
<dc:title><![CDATA[Transcriptomic profiling of Candidatus Liberibacter asiaticus in different citrus tissues reveals novel insights into Huanglongbing pathogenesis]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-09-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.09.19.613839v1?rss=1">
<title>
<![CDATA[
A helper NLR targets organellar membranes to trigger immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.09.19.613839v1?rss=1"
</link>
<description><![CDATA[
Upon activation, plant NLR immune receptors are known to assemble into oligomeric resistosomes that insert into the plasma membrane, forming Ca2+-permeable channels and triggering immunity. Here, we show that the RPW8-like coiled-coil (CCR-) NLR NRG1 primarily targets organelles instead of the plasma membrane. Unlike canonical CC-NLRs, activated NRG1 accumulates at the chloroplast envelope and channels stromal Ca2+ into the cytosol. AlphaFold modeling of the NRG1 resistosome reveals an unusually long N-terminal membrane-insertion structure that would span the double chloroplast membranes. Nanobody-mediated relocalization shows functional membrane specificity: chloroplast trapping abolishes activity of the canonical helper CC-NLR NRC4 but not NRG1. NRG1 orthologs, from non-flowering lineages to angiosperms, target chloroplasts, suggesting that organelle-centered defense dates back to at least [~]360 million years. We propose that coiled-coil NLR diversification has enabled compartment-specific immune signaling to capture diverse Ca2+ stores.
]]></description>
<dc:creator>Ibrahim, T.</dc:creator>
<dc:creator>Yuen, E. L. H.</dc:creator>
<dc:creator>Wang, H.-Y.</dc:creator>
<dc:creator>King, F. J.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Vuolo, C.</dc:creator>
<dc:creator>Adamkova, V.</dc:creator>
<dc:creator>Castel, B.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:date>2024-09-22</dc:date>
<dc:identifier>doi:10.1101/2024.09.19.613839</dc:identifier>
<dc:title><![CDATA[A helper NLR targets organellar membranes to trigger immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-09-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.11.24.625045v1?rss=1">
<title>
<![CDATA[
Can AI modelling of protein structures distinguish between sensor and helper NLR immune receptors? 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.11.24.625045v1?rss=1"
</link>
<description><![CDATA[
NLR immune receptors can be functionally organized in genetically linked sensor-helper pairs. However, methods to categorize paired NLRs remain limited, primarily relying on the presence of non-canonical domains in some sensor NLRs. Here, we propose that the AI system AlphaFold 3 can classify paired NLR proteins into sensor or helper categories based on predicted structural characteristics. Helper NLRs showed higher AlphaFold 3 confidence scores than sensors when modelled in oligomeric configurations. Furthermore, funnel-shaped structures--essential for activating immune responses--were reliably predicted in helpers but not in sensors. Applying this method to uncharacterized NLR pairs from rice, we found that AlphaFold 3 can differentiate between putative sensors and helpers even when both proteins lack non-canonical domain annotations. These findings suggest that AlphaFold 3 offers a new approach to categorize NLRs and enhances our understanding of the functional configurations in plant immune systems, even in the absence of non-canonical domain annotations.
]]></description>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Terauchi, R.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:date>2024-11-26</dc:date>
<dc:identifier>doi:10.1101/2024.11.24.625045</dc:identifier>
<dc:title><![CDATA[Can AI modelling of protein structures distinguish between sensor and helper NLR immune receptors?]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-11-26</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.12.03.626388v1?rss=1">
<title>
<![CDATA[
Conserved effectors underpin the virulence of liverwort-isolated Pseudomonas in divergent plants 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.12.03.626388v1?rss=1"
</link>
<description><![CDATA[
Plant pathogenic Pseudomonas species naturally antagonize a diverse range of flowering plants. While emerging research demonstrates that isolates belonging to the P. syringae species complex colonize diverse hosts, the extent to which these bacteria naturally infect non-flowering plants like the model liverwort Marchantia polymorpha remains unclear. Here, we identify natural associations between Pseudomonas viridiflava and the liverwort Marchantia polymorpha. Pseudomonas bacteria isolated from diseased liverworts in the wild successfully re-infected M. polymorpha in pure culture conditions, producing high in planta bacterial densities and causing prominent tissue maceration. Comparative genomic analysis of Marchantia-associated P. viridiflava identified core virulence machinery like the type-III secretion system (T3SS) and conserved effectors (AvrE and HopM1) that were essential for liverwort infection. Disease assays performed in Nicotiana benthamiana further confirmed that liverwort-associated P. viridiflava infect flowering plants in an effector-dependent manner. Our work highlights P. viridiflava as an effective broad host pathogen that relies on conserved virulence factors to manipulate evolutionarily divergent host plants.
]]></description>
<dc:creator>Robinson, K.</dc:creator>
<dc:creator>Buric, L.</dc:creator>
<dc:creator>Grenz, K.</dc:creator>
<dc:creator>Chia, K.-S.</dc:creator>
<dc:creator>Hulin, M. T.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Carella, P.</dc:creator>
<dc:date>2024-12-03</dc:date>
<dc:identifier>doi:10.1101/2024.12.03.626388</dc:identifier>
<dc:title><![CDATA[Conserved effectors underpin the virulence of liverwort-isolated Pseudomonas in divergent plants]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-12-03</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.12.08.627391v1?rss=1">
<title>
<![CDATA[
Chitin soil amendment triggers systemic plant disease resistance through enhanced pattern-triggered immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.12.08.627391v1?rss=1"
</link>
<description><![CDATA[
Chitin triggers localised and systemic plant immune responses, making it a promising treatment for sustainable disease resistance. However, the precise molecular mechanisms underlying chitin-induced systemic effects in plants remain unknown. In this study, we investigated the effects of soil amendment with crab chitin flakes (hereafter chitin) on pattern-triggered immunity (PTI) and systemic disease resistance in various plant species. We found that soil amendment with chitin potentiates PTI and disease resistance against the bacterial pathogen Pseudomonas syringae pv. tomato DC3000 in lettuce, tomato, and Arabidopsis as well as against the fungal pathogen Blumeria graminis causing powdery mildew in wheat. Using micrografting in Arabidopsis, we demonstrated that this systemic effect is dependent on active chitin perception in the roots. We also showed that induced systemic resistance (ISR) and pattern-recognition receptors (PRRs)/co-receptors, but not systemic acquired resistance (SAR), are involved in the systemic effects triggered by chitin soil amendment. This systemic effect correlated with the transcriptional up-regulation of key PTI components in distal leaves upon chitin soil amendment. Notably, chitin-triggered systemic immunity was independent of microbes present in soil or chitin flakes. Together, these findings contribute to a better understanding of chitin-triggered systemic immunity, from active chitin perception in roots to the potentiation of PTI in the leaves, ultimately priming plants to mount enhanced defense responses against pathogen attacks. Our study provides valuable insights into the molecular mechanisms of chitin soil amendment and resulting induced immunity, and highlights its potential use for sustainable crop protection strategies.
]]></description>
<dc:creator>Makechemu, M.</dc:creator>
<dc:creator>Goto, Y.</dc:creator>
<dc:creator>Zbinden, H.</dc:creator>
<dc:creator>Widrig, V.</dc:creator>
<dc:creator>Keller, B.</dc:creator>
<dc:creator>zipfel, c.</dc:creator>
<dc:date>2024-12-10</dc:date>
<dc:identifier>doi:10.1101/2024.12.08.627391</dc:identifier>
<dc:title><![CDATA[Chitin soil amendment triggers systemic plant disease resistance through enhanced pattern-triggered immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-12-10</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.11.05.622083v1?rss=1">
<title>
<![CDATA[
The phosphatase PP2C12 is a negative player in LRX-RALF-FER-mediated cell wall integrity sensing 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.11.05.622083v1?rss=1"
</link>
<description><![CDATA[
Plants have evolved an elaborate cell wall integrity (CWI) sensing system to monitor and modify cell wall formation. LRR-extensins (LRXs) are cell wall-anchored proteins that bind RAPID ALKALINIZATION FACTOR (RALF) peptide hormones and induce compaction of cell wall structures. At the same time, LRXs form a signaling platform with RALFs and the transmembrane receptor kinase FERONIA (FER) as a means to relay changes in CWI to the protoplast. LRX1 of Arabidopsis thaliana is predominantly expressed in root hairs and lrx1 mutants develop defective root hairs. Here, we identify a regulator of LRX1-RALF-FER signaling as a suppressor of the lrx1 root hair phenotype. The repressor of lrx1_23 (rol23) gene encodes PP2C12, a type 2C phosphatase of clade H that interacts with FER and dephosphorylates Thr696 in the FER activation loop in vitro. The LRX1-related function of PP2Cs appears clade H-specific and was not observed for other PP2Cs investigated. Collectively, our data suggest that LRX1 acts upstream of the RALF1-FER signaling module and PP2C12 has an inhibitory activity via modulating FER activity to fine-tune CWI signaling.
]]></description>
<dc:creator>Hou, X.</dc:creator>
<dc:creator>Bender, K. W.</dc:creator>
<dc:creator>Guerin, A.</dc:creator>
<dc:creator>Kadler, G.</dc:creator>
<dc:creator>Gupta, S.</dc:creator>
<dc:creator>Haefliger, M.</dc:creator>
<dc:creator>Diet, A.</dc:creator>
<dc:creator>Roffler, S.</dc:creator>
<dc:creator>Campanini, D.</dc:creator>
<dc:creator>Wicker, T.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Ringli, C.</dc:creator>
<dc:date>2024-11-06</dc:date>
<dc:identifier>doi:10.1101/2024.11.05.622083</dc:identifier>
<dc:title><![CDATA[The phosphatase PP2C12 is a negative player in LRX-RALF-FER-mediated cell wall integrity sensing]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-11-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.01.26.634911v1?rss=1">
<title>
<![CDATA[
The dominant lineage of Phakopsora pachyrhizi in the United States of America does not have a Brazilian origin 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.01.26.634911v1?rss=1"
</link>
<description><![CDATA[
O_LIAsian soybean rust (ASR), caused by the obligate biotrophic fungus, Phakopsora pachyrhizi, was first reported in the continental United States of America (USA) in 2004 and over the years has been of concern to soybean production in the USA. The prevailing hypothesis is that P. pachyrhizi spores were introduced into the USA via hurricanes originating from South America, particularly Hurricane Ivan.
C_LIO_LITo investigate the genetic diversity and global population structure of P. pachyrhizi, we employed exome-capture based sequencing on 84 field isolates collected from different geographic regions worldwide. We compared the gene-encoding regions from all these field isolates and found that four major haplotypes are prevalent worldwide. Here, we provide genetic evidence supporting multiple incursions that have led to the currently established P. pachyrhizi population of the USA. Phylogenetic analysis of mitochondrial genes further supports this hypothesis.
C_LIO_LINotably, we observed limited genetic diversity in P. pachyrhizi populations in Brazil, suggesting a clonal population structure in that country that contrasts to populations from the USA and Africa.
C_LIO_LIThis study provides the first comprehensive characterization of P. pachyrhizi population structures defined by genetic evidence from populations across major soybean growing regions.
C_LI
]]></description>
<dc:creator>Ferreira, E. G. C.</dc:creator>
<dc:creator>Inoue, Y.</dc:creator>
<dc:creator>Murithi, H. M.</dc:creator>
<dc:creator>Nardwattanawong, T.</dc:creator>
<dc:creator>Cheema, J.</dc:creator>
<dc:creator>Grootens, R.</dc:creator>
<dc:creator>Paes, S. A.</dc:creator>
<dc:creator>Mahuku, G.</dc:creator>
<dc:creator>Joosten, M. H. A. J.</dc:creator>
<dc:creator>Hartman, G.</dc:creator>
<dc:creator>Yamaoka, Y.</dc:creator>
<dc:creator>Brommonschenkel, S. H.</dc:creator>
<dc:creator>van Esse, H. P.</dc:creator>
<dc:creator>Gupta, Y. K.</dc:creator>
<dc:date>2025-01-27</dc:date>
<dc:identifier>doi:10.1101/2025.01.26.634911</dc:identifier>
<dc:title><![CDATA[The dominant lineage of Phakopsora pachyrhizi in the United States of America does not have a Brazilian origin]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-01-27</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.12.24.629987v1?rss=1">
<title>
<![CDATA[
A Witches' Broom Phytoplasma effector induces stunting by stabilizing a bHLH transcription factor in plants 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.12.24.629987v1?rss=1"
</link>
<description><![CDATA[
O_LIPhytoplasmas are specialized phloem-limited bacteria that cause diseases on various crops resulting in significant agricultural losses. This research focuses on the jujube Witches Broom (JWB) phytoplasma and investigates the host-manipulating activity of the effector SJP39.
C_LIO_LIWe found that SJP39 directly interacts with the plant transcription factor bHLH87 in the nuclei. SJP39 stabilizes the bHLH87 homologs in A. thaliana and jujube, leading to growth defects in the plants.
C_LIO_LITranscriptomic analysis indicates that SJP39 affects the gibberellin (GA) pathway in jujube. We further demonstrate that ZjbHLH87 regulates GA signalling as a negative regulator and SJP39 enhances this regulation.
C_LIO_LIThe research offers important insights into the pathogenesis of JWB disease and identified SJP39 as a virulence factor that can contribute to the growth defects caused by JWB phytoplasma infection. These findings open new opportunities to manage JWB and other phytoplasma diseases.
C_LI
]]></description>
<dc:creator>Yang, S.</dc:creator>
<dc:creator>Lovelace, A.</dc:creator>
<dc:creator>Yuan, Y.</dc:creator>
<dc:creator>Nie, H.</dc:creator>
<dc:creator>Chen, W.</dc:creator>
<dc:creator>Gao, Y.</dc:creator>
<dc:creator>Bo, W. B.</dc:creator>
<dc:creator>Nagel, D. H.</dc:creator>
<dc:creator>Pang, X.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:date>2024-12-24</dc:date>
<dc:identifier>doi:10.1101/2024.12.24.629987</dc:identifier>
<dc:title><![CDATA[A Witches' Broom Phytoplasma effector induces stunting by stabilizing a bHLH transcription factor in plants]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-12-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.02.25.639832v1?rss=1">
<title>
<![CDATA[
A hierarchical immune receptor network in lettuce reveals contrasting patterns of evolution in sensor and helper NLRs 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.02.25.639832v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding domain and leucine-rich repeat immune receptors (NLRs) are known for their rapid evolution, even at the intraspecific level, yet the rates of evolution differ significantly across various NLR classes. Within the NRC (NLR Required for Cell Death) network, NLRs operate in complex sensor-helper configurations to confer immunity against a diverse array of pathogens, particularly in Asterids. While helper NLRs are typically conserved and evolve slowly, sensor NLRs tend to evolve more rapidly. However, the functional connections between slow and fast-evolving NLRs remain poorly understood, notably in important crop species. We conducted a comparative analysis of NLRs across 40 Solanales and 29 Asterales genomes to explore NRC network expansion and diversification within the less-studied Asterales order. Our findings reveal that the NRC network has expanded less in Asterales compared to Solanales. We functionally validated a minimal Asterales NRC network with 2 helpers and 9 sensors in common lettuce (Lactuca sativa). Through selection and diversification analysis and structural modeling of NRC helper and sensor subclades in the Lactuca genus, we found varying evolutionary diversification rates between NRC helpers and sensors. We found a correlation between sensor diversification rates and helper dependency, with sensors reliant on a phylogenetically conserved helpers experiencing limited diversification pressure. Our results highlight the lineage- and function-specific evolution of the NRC network, offering insights into the evolutionary pressures shaping plant immune receptor networks.
]]></description>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Sakai, T.</dc:creator>
<dc:creator>Posbeyikian, A.</dc:creator>
<dc:creator>Frijters, R.</dc:creator>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Adachi, H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:date>2025-02-25</dc:date>
<dc:identifier>doi:10.1101/2025.02.25.639832</dc:identifier>
<dc:title><![CDATA[A hierarchical immune receptor network in lettuce reveals contrasting patterns of evolution in sensor and helper NLRs]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-02-25</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.07.14.664264v1?rss=1">
<title>
<![CDATA[
A plant pathogen effector blocks stepwise assembly of a helper NLR resistosome 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.07.14.664264v1?rss=1"
</link>
<description><![CDATA[
Helper NLRs function as central nodes in plant immune networks. Upon activation, they oligomerize into inflammasome-like resistosomes to initiate immune signaling, yet the dynamics of resistosome assembly remain poorly understood. Here, we show that the virulence effector AVRcap1b from the Irish potato famine pathogen Phytophthora infestans suppresses immune activation by directly engaging oligomerization intermediates of the tomato helper NLR SlNRC3. Cryo-EM structures of SlNRC3 in AVRcap1b-bound and unbound states reveal that AVRcap1b bridges multiple protomers, stabilizing a stalled intermediate and preventing formation of a functional resistosome. Leveraging AVRcap1b as a molecular tool, we also capture an additional SlNRC3 resistosome intermediate showing that assembly proceeds in a stepwise manner from dissociated monomers. These findings uncover a previously unrecognized vulnerability in NLR activation and reveal a pathogen strategy that disrupts immune complex assembly. This work advances mechanistic understanding of resistosome formation and uncovers a previously unrecognized facet of pathogen-plant coevolution.
]]></description>
<dc:creator>Seager, B. A.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Hou, L.-Y.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Madhuprakash, J.</dc:creator>
<dc:date>2025-07-14</dc:date>
<dc:identifier>doi:10.1101/2025.07.14.664264</dc:identifier>
<dc:title><![CDATA[A plant pathogen effector blocks stepwise assembly of a helper NLR resistosome]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-07-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.07.07.663532v1?rss=1">
<title>
<![CDATA[
β-sheet stabilization of the island domain underlies ligand-induced LRR-RP activation of plant immune signaling 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.07.07.663532v1?rss=1"
</link>
<description><![CDATA[
Leucine-rich repeat (LRR) receptor kinases (RKs) and receptor proteins (RPs) are important classes of plant pattern recognition receptors (PRRs) activating pattern-triggered immunity. While both classical and AI-based structural approaches have recently provided crucial insights into ligand-LRR-RK binding mechanisms, our understanding of ligand perception by LRR-RPs remains limited. In contrast to LRR-RKs, many LRR-RPs typically embed one or more loopout regions in their extracellular domains that are crucial for functionality. Here, we employed an AI-based approach to reveal a novel ligand-binding mechanism shared by the Arabidopsis LRR-RPs RLP23 and RLP42 - the PRRs for the short peptide ligands nlp20 and pg13, derived from NECROSIS- AND ETHYLENE-INDUCING PEPTIDE 1-like proteins (NLPs) and fungal endopolygalacturonases (PGs), respectively. This mechanism relies on a {beta}-strand interaction with the N-terminal part of the island domain (ID) loopout, which adopts an antiparallel {beta}-sheet conformation. Additionally, we investigated the larger and more complex binding interface of RLP32 - the PRR for proteobacterial TRANSLATION INITIATION FACTOR 1 (IF1), a folded protein ligand that requires its tertiary structure for recognition. Finally, we describe a mechanistic role of the ID for co-receptor recruitment conserved across LRR-RPs. Together, our results shed light on the ligand-binding mechanisms and receptor complex formation of this important class of PRRs. This opens avenues for a molecular understanding of the plant-pathogen co-evolution, as well as the engineering of plant immune receptors for crop disease resistance.
]]></description>
<dc:creator>Snoeck, S.</dc:creator>
<dc:creator>Zhang, L.</dc:creator>
<dc:creator>Studer, V.</dc:creator>
<dc:creator>Kim, G.</dc:creator>
<dc:creator>Fernandez-Fernandez, A. D.</dc:creator>
<dc:creator>Nuernberger, T.</dc:creator>
<dc:creator>zipfel, c.</dc:creator>
<dc:date>2025-07-09</dc:date>
<dc:identifier>doi:10.1101/2025.07.07.663532</dc:identifier>
<dc:title><![CDATA[β-sheet stabilization of the island domain underlies ligand-induced LRR-RP activation of plant immune signaling]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-07-09</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.03.11.642614v1?rss=1">
<title>
<![CDATA[
The autoactivity of tomato helper NLR immune proteins of the NRC clade is unaltered in prf mutants of Nicotiana benthamiana 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.03.11.642614v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding domain and leucine-rich repeat immune receptors (NLRs) can function in networks of sensors and helpers to induce hypersensitive cell death and immunity against pathogens. The tomato sensor NLR Prf guards the Pto kinase from AvrPto and AvrPtoB effector perturbation and activates the downstream helpers NRC2 and NRC3. Prf is conserved across the Solanaceae and its ortholog in the model species Nicotiana benthamiana is also required for detection of AvrPto/AvrPtoB function on Pto. A recent study reported that cell death induction after transient expression of an autoactive mutant of tomato NRC3 is abolished upon RNAi silencing of Prf in N. benthamiana. Here we generated loss-of-function prf mutants in N. benthamiana and demonstrate that autoactive mutants of eight canonical tomato NRCs (NRC0, NRC1, NRC2, NRC3, NRC4a, NRC4b, NRC6, and NRC7) still induce hypersensitive cell death when expressed transiently in the prf mutant background. Autoactive tomato NRCs also triggered cell death when expressed in lettuce (Lactuca sativa), an Asteraceae plant that does not have a Prf ortholog. These results confirm a unidirectional dependency of sensors and helpers in the NRC network and underscore the value of the N. benthamiana and lettuce model systems for studying functional relationships between paired and networked NLRs.
]]></description>
<dc:creator>Luedke, D.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Harant, A.</dc:creator>
<dc:creator>Wu, C.-H.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2025-03-13</dc:date>
<dc:identifier>doi:10.1101/2025.03.11.642614</dc:identifier>
<dc:title><![CDATA[The autoactivity of tomato helper NLR immune proteins of the NRC clade is unaltered in prf mutants of Nicotiana benthamiana]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-03-13</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.04.11.646618v1?rss=1">
<title>
<![CDATA[
Recognition-dependent activation of the RRS1-R/RPS4 immune receptor complex 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.04.11.646618v1?rss=1"
</link>
<description><![CDATA[
The Arabidopsis TIR-NLR immune receptors RPS4 and RRS1 function together to enable recognition of multiple effector proteins including AvrRps4 and PopP2. We show here that both in the presence and absence of effector, RPS4 and RRS1 form an oligomer that does not change in size upon effector provision. Oligomer formation involves interactions between the RPS4 and RRS1 TIR domains and requires nucleotide binding capacity in RPS4. RPS4 mutants that lose TIR domain NADase activity abrogate immune activation but retain oligomerization. A cysteine residue in the RPS4 LRR domain contributes to oligomer stabilization. We propose that upon effector recognition, conformational changes in the complex relieve inhibition of RPS4 TIR domains by RRS1 TIR domains, enabling proximity between RPS4 TIR domains to create NADase activity.
]]></description>
<dc:creator>Ahn, H.-K.</dc:creator>
<dc:creator>Guo, G.</dc:creator>
<dc:creator>Sklenar, J.</dc:creator>
<dc:creator>Keh, S. P. Y.</dc:creator>
<dc:creator>Huh, S. U.</dc:creator>
<dc:creator>Hulin, M. T.</dc:creator>
<dc:creator>Burdett, H.</dc:creator>
<dc:creator>Sindalovskaya, M.</dc:creator>
<dc:creator>Choi, J.</dc:creator>
<dc:creator>Mukhi, N.</dc:creator>
<dc:creator>Zhao, H.</dc:creator>
<dc:creator>Knorr, L.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2025-04-14</dc:date>
<dc:identifier>doi:10.1101/2025.04.11.646618</dc:identifier>
<dc:title><![CDATA[Recognition-dependent activation of the RRS1-R/RPS4 immune receptor complex]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-04-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.04.25.650432v1?rss=1">
<title>
<![CDATA[
Two genetically linked Arabidopsis TIR-type NLRs are required for immunity and interact with NLRs encoded in a segmentally duplicated genomic region 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.04.25.650432v1?rss=1"
</link>
<description><![CDATA[
Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors detect pathogen-secreted effectors inside host cells and induce a robust immune response, typically involving hypersensitive cell death. NLR genes are often genetically linked and can function as pairs or within larger NLR networks. We previously showed that the truncated Toll/Interleukin-1 Receptor (TIR)-type NLR TIR-NB13 (TN13) is required for resistance of Arabidopsis to Pseudomonas syringae pv. tomato (Pst) DC3000 lacking the type-III effector proteins AvrPto and AvrPtoB. TN13 is genetically linked to a full length TIR-NB-LRR (TNL) gene on chromosome 3. Here, we show that TN13, and its genetically linked TNL both localize to the ER membrane via N-terminal transmembrane domains, are required for resistance to Pst DC3000 ({Delta}AvrPto/AvrPtoB) and interact with each other in transient expression assays in Nicotiana benthamiana. In contrast to TN13, the full length TNL, which we named TN13-INTERACTING TNL1 (TNT1), induces an autoactive cell death response when expressed in N. benthamiana that depends on an atypical MHV motif in its NB-ARC domain, as well as the EDS1/SAG101/NRG1 module. TN13 and TNT1 furthermore interact with phylogenetically related NLRs encoded by a segmentally duplicated region on chromosome 5. Our data suggest that both TN13 and the genetically linked TNT1 could be part of a larger TIR-type NLR immune regulatory network, in which TNT1 contributes to basal immunity and might function as an autoactive death switch to induce cell death upon pathogen detection.

SIGNIFICANCE STATEMENTThe ER membrane localized truncated TIR-NLR TN13 and the genomically linked full length TNL TNT1 are required for plant disease resistance and form heteromeric associations with phylogenetically related NLRs, encoded by a segmentally duplicated chromosomal region.
]]></description>
<dc:creator>Luedke, D.</dc:creator>
<dc:creator>Yan, Q.</dc:creator>
<dc:creator>Zirngibl, M.-E.</dc:creator>
<dc:creator>Roth, C.</dc:creator>
<dc:creator>Klenke, M.</dc:creator>
<dc:creator>Gunkel, A.</dc:creator>
<dc:creator>Wiermer, M.</dc:creator>
<dc:date>2025-04-26</dc:date>
<dc:identifier>doi:10.1101/2025.04.25.650432</dc:identifier>
<dc:title><![CDATA[Two genetically linked Arabidopsis TIR-type NLRs are required for immunity and interact with NLRs encoded in a segmentally duplicated genomic region]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-04-26</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.05.22.655486v1?rss=1">
<title>
<![CDATA[
MIK2 clade receptor function in perception of a Fusarium-derived elicitor is conserved among different plant families 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.05.22.655486v1?rss=1"
</link>
<description><![CDATA[
Plants constantly monitor their environment to adapt to potential threats to their health and fitness. This involves cell-surface receptors that can detect conserved microbe-associated molecular patterns (MAMPs) or endogenous immunogenic signals, initiating signaling pathways to induce broad-spectrum disease resistance, known as pattern-triggered immunity (PTI). In Arabidopsis thaliana, the leucine-rich repeat receptor kinase (LRR-RK) MIK2 is an exceptionally versatile receptor involved in the perception of the vast family of Brassicales-specific endogenous SCOOP peptides as well as potential MAMPs derived from Fusarium and related fungi. Although only plant species belonging to the order of Brassicales encode genes for SCOOP peptides and show SCOOP-responsiveness, the Fusarium-derived elicitor fraction also induces PTI responses in plants from other lineages. In this study, we demonstrate that Fusarium elicitor-responsiveness and proteins belonging to the MIK2-clade are widely conserved among seed plants. We identified a MIK2-clade protein from tomato, which shares properties of AtMIK2 in the perception of the Fusarium elicitor but not of SCOOP peptides. Tomato mutants lacking the receptor show compromised PTI responses to the fungal elicitor and enhanced susceptibility to infection by Fusarium oxysporum. Our data provide insights into the evolutionary trajectory of MIK2 as a multifunctional receptor involved in plant immunity.
]]></description>
<dc:creator>Maroschek, J.</dc:creator>
<dc:creator>Roesgen, Y.</dc:creator>
<dc:creator>Roessner, C.</dc:creator>
<dc:creator>Snoeck, S.</dc:creator>
<dc:creator>Schwechheimer, C.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Hueckelhoven, R.</dc:creator>
<dc:date>2025-05-23</dc:date>
<dc:identifier>doi:10.1101/2025.05.22.655486</dc:identifier>
<dc:title><![CDATA[MIK2 clade receptor function in perception of a Fusarium-derived elicitor is conserved among different plant families]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-05-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.06.02.657414v1?rss=1">
<title>
<![CDATA[
New alleles of Arabidopsis BIK1 reinforce its predominant role in pattern-triggered immunity and caution interpretations of other reported functions 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.06.02.657414v1?rss=1"
</link>
<description><![CDATA[
The receptor-like cytoplasmic kinase BIK1 and its close homolog PBL1 have been widely recognized as central components of plant immunity. However, most genetic studies of BIK1 and PBL1 functions were carried out with single T-DNA insertional mutant alleles. Some phenotypes observed in these mutants, e.g. autoimmunity, have been difficult to reconcile with the proposed role of BIK1 and PBL1 in pattern-triggered immunity. In this study, we generated multiple new alleles of bik1 and pbl1 by CRISPR-Cas9-based gene editing and systematically analyzed these mutants alongside existing T-DNA insertional lines. These analyses reinforced the central role of BIK1 and PBL1 in pattern-triggered immunity mediated by both receptor kinases and receptor-like proteins. At the same time, however, we revealed several pleiotropic phenotypes associated with T-DNA insertions that are not necessarily linked to loss of BIK1 or PBL1 function. Further analyses of newly generated bik1 pbl1 double mutants uncovered an even greater contribution of these kinases to immune signaling and disease resistance than previously appreciated. These findings clarify longstanding ambiguities surrounding BIK1 and PBL1 functions.
]]></description>
<dc:creator>Song, B.</dc:creator>
<dc:creator>Choi, S.</dc:creator>
<dc:creator>Kong, L.</dc:creator>
<dc:creator>Kim, S.-I.</dc:creator>
<dc:creator>Fliegmann, J.</dc:creator>
<dc:creator>Li, X.</dc:creator>
<dc:creator>DeFalco, T. A.</dc:creator>
<dc:creator>Hu, M.</dc:creator>
<dc:creator>Li, M.</dc:creator>
<dc:creator>Zhao, Y.</dc:creator>
<dc:creator>Wang, H.</dc:creator>
<dc:creator>Shan, L.</dc:creator>
<dc:creator>Nuernberger, T.</dc:creator>
<dc:creator>He, P.</dc:creator>
<dc:creator>zipfel, c.</dc:creator>
<dc:creator>Zhou, J.-M.</dc:creator>
<dc:date>2025-06-06</dc:date>
<dc:identifier>doi:10.1101/2025.06.02.657414</dc:identifier>
<dc:title><![CDATA[New alleles of Arabidopsis BIK1 reinforce its predominant role in pattern-triggered immunity and caution interpretations of other reported functions]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-06-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.06.02.656948v1?rss=1">
<title>
<![CDATA[
Defense-Suppressive Fragments of RIN4 generated by AvrRpt2 Participate in NDR1-dependent Activation of RPS2 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.06.02.656948v1?rss=1"
</link>
<description><![CDATA[
Plant nucleotide-binding, leucine-rich-repeat (NLR) immune receptors recognize pathogen effectors and activate immunity. The NLR RPS2 recognizes AvrRpt2, a Pseudomonas effector that promotes virulence by proteolytically cleaving a membrane-tethered host protein, RIN4. RIN4 cleavage by AvrRpt2 generates fragments that activate RPS2. A model for RPS2 activation by RIN4 destruction is consistent with the ectopic activity of RPS2 in plants lacking RIN4 but does not explain the link between AvrRpt2s virulence activity and RPS2 activation. We found that non-membrane-tethered RIN4 derivatives are potent cytosolic activators of RPS2. Activation of RPS2 by these RIN4 derivatives, like AvrRpt2-induced activation, and unlike ectopic activation in the absence of RIN4, requires the defense signaling protein NDR1. Cleavage products of RIN4 produced by AvrRpt2 play contrasting roles in the activation of RPS2, with the membrane-tethered C-terminal fragment suppressing RPS2 and the non-membrane-tethered internal fragment, dependent on compatibility with the C-terminal fragment, overcoming its suppression of RPS2.

HighlightsO_LINon-membrane tethered derivatives of RIN4 activate RPS2-induced cell death
C_LIO_LIActivation of RPS2 by non-membrane-tethered derivatives of RIN4 requires NDR1
C_LIO_LIAvrRpt2-induced cleavage fragments of RIN4 play contrasting roles in RPS2 activation
C_LI
]]></description>
<dc:creator>Afzal, A. J.</dc:creator>
<dc:creator>Alam, M.</dc:creator>
<dc:creator>Huang, J.</dc:creator>
<dc:creator>Agha, M.</dc:creator>
<dc:creator>Da Cunha, L.</dc:creator>
<dc:creator>Iqbal Rai, M.</dc:creator>
<dc:creator>Tahir, J.</dc:creator>
<dc:creator>Jamroze, A.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Mackey, D.</dc:creator>
<dc:date>2025-06-04</dc:date>
<dc:identifier>doi:10.1101/2025.06.02.656948</dc:identifier>
<dc:title><![CDATA[Defense-Suppressive Fragments of RIN4 generated by AvrRpt2 Participate in NDR1-dependent Activation of RPS2]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-06-04</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.06.28.662111v1?rss=1">
<title>
<![CDATA[
Cell-type-specific execution of effector-triggered immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.06.28.662111v1?rss=1"
</link>
<description><![CDATA[
Effector-triggered immunity (ETI) is a central component of host defense, but whether all cell types execute ETI similarly remains unknown. We combined chemically imposed immune activation with single-cell transcriptomics to profile ETI responses across all leaf cell types in Arabidopsis. Despite uniform ETI perception, we find striking divergence between transcriptional outputs: a core set of defense genes is broadly induced, while distinct cell types activate specialized immune modules. We infer that downstream immune execution is shaped not only by immune receptor activation, but also by cell identity and its associated transcriptional regulatory context, including local transcription factor availability and chromatin accessibility. We further demonstrate that transcriptional regulators preferentially induced in epidermal cells are required to restrict invasion by non-adapted pathogens. Their absence permits pathogen entry into deeper tissues despite intact recognition, revealing a spatial division of immune functions. Our findings uncover a layered immune architecture in plants, challenges the assumption of uniform immune execution, and provides a framework for exploring cell-type-specific resistance logic in multicellular hosts.
]]></description>
<dc:creator>Chhillar, H.</dc:creator>
<dc:creator>Jo, L.</dc:creator>
<dc:creator>Redkar, A.</dc:creator>
<dc:creator>Kajala, K.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Ding, P.</dc:creator>
<dc:date>2025-07-01</dc:date>
<dc:identifier>doi:10.1101/2025.06.28.662111</dc:identifier>
<dc:title><![CDATA[Cell-type-specific execution of effector-triggered immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-07-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.07.06.663370v1?rss=1">
<title>
<![CDATA[
An effector from the potato late blight pathogen bridges ENTH-domain protein TOL9a to an activated helper NLR to suppress immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.07.06.663370v1?rss=1"
</link>
<description><![CDATA[
Pathogens counteract central nodes of NLR immune receptor networks to suppress immunity. However, the mechanisms by which pathogens hijack helper NLR pathways are poorly understood. Here, we show that an effector from the potato late blight pathogen Phytophthora infestans bridges the host protein NbTOL9a, a putative member of the host ESCRT pathway, to a helper NLR to suppress immunity. In this work, we solved the crystal structure of the RXLR-LWY effector AVRcap1b in complex with the ENTH domain of NbTOL9a. The structure revealed that unlike other RXLR-LWY effectors, AVRcap1b has a novel L-shaped fold that defines a new structural family of effectors in the Phytophthora genus. Moreover, we defined the AVRcap1b/NbTOL9a binding interface and designed effector mutants that dont bind NbTOL9a, impairing immune suppression. This indicates that ENTH binding is required for full virulence activity of this effector. Lastly, we show that AVRcap1b associates specifically with activated NbNRC2 independently of NbTOL9a binding. This suggests that the effector functions as a bridge that interconnects NbNRC2 with the NbTOL9a pathway. These results illustrate an unprecedented pathogen mechanism to hijack helper NLR pathways and suppress immunity.
]]></description>
<dc:creator>Madhuprakash, J.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Harvey, M.</dc:creator>
<dc:creator>Bentham, A. R.</dc:creator>
<dc:creator>Seager, B. A.</dc:creator>
<dc:creator>Yuen, E. L. H.</dc:creator>
<dc:creator>De la Concepcion, J. C.</dc:creator>
<dc:creator>Lawson, D. M.</dc:creator>
<dc:creator>Stevenson, C. E. M.</dc:creator>
<dc:creator>Vergara-Cruces, A.</dc:creator>
<dc:creator>Derevnina, L.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:date>2025-07-08</dc:date>
<dc:identifier>doi:10.1101/2025.07.06.663370</dc:identifier>
<dc:title><![CDATA[An effector from the potato late blight pathogen bridges ENTH-domain protein TOL9a to an activated helper NLR to suppress immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-07-08</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.07.20.665670v1?rss=1">
<title>
<![CDATA[
A conserved small RNA-generating gene cluster undergoes sequence diversification and contributes to plant immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.07.20.665670v1?rss=1"
</link>
<description><![CDATA[
Small RNA-mediated gene silencing contributes to plant immunity. The secondary small interfering RNA (siRNA) pathway promotes defense by silencing target genes in invading fungal and oomycete pathogens. Many secondary siRNAs derive from transcripts potentially encoding pentatricopeptide repeat (PPR) proteins. Here, we report that siRNA production is an ancient function of an evolutionarily conserved clade of PPR genes that undergo extensive within-species diversification. In Arabidopsis thaliana, siRNA-source PPRs are physically clustered in one locus on Chromosome 1. These sequences are diversified through gene duplication followed by sequence diversification as well as accumulation of high-impact variations including pseudogenization. This diversity leads to the accumulation of a diverse PPR-siRNA pool, consistent with an engagement in a co-evolutionary arms race with the pathogens. This study defines siRNA-producing PPRs as a family of defense genes and highlights the potential of PPR-siRNA-based engineering for enhancing broad-spectrum disease resistance.
]]></description>
<dc:creator>Feng, L.</dc:creator>
<dc:creator>Hou, Y.</dc:creator>
<dc:creator>Toghani, A.</dc:creator>
<dc:creator>Wang, Z.</dc:creator>
<dc:creator>Tang, B.</dc:creator>
<dc:creator>Atkinson, N.</dc:creator>
<dc:creator>Li, H.</dc:creator>
<dc:creator>Qiao, Y.</dc:creator>
<dc:creator>Wang, Y.</dc:creator>
<dc:creator>Hua, J.</dc:creator>
<dc:creator>Zhai, J.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:date>2025-07-21</dc:date>
<dc:identifier>doi:10.1101/2025.07.20.665670</dc:identifier>
<dc:title><![CDATA[A conserved small RNA-generating gene cluster undergoes sequence diversification and contributes to plant immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-07-21</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.08.12.669671v1?rss=1">
<title>
<![CDATA[
Rewinding the tape: historical contingency and functional constraints have shaped the evolution of APikL virulence effectors in the blast fungus 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.08.12.669671v1?rss=1"
</link>
<description><![CDATA[
Protein evolution is influenced by historical contingencies and functional constraints, but their combined impact on rapidly diversifying pathogen virulence effectors remains poorly understood. Here, we combined ancestral state reconstructions and functional assays to recapitulate the evolution of the MAX-fold effector protein APikL2 of the plant pathogenic blast fungus Magnaporthe (syn. Pyricularia) oryzae, focusing on the ancestral and functionally critical amino acid residue D66 (Asp, Codon: GAT). "Rewinding the tape" experiments based on ancestral sequence resurrection revealed that, out of the seven potential amino acid substitutions derived from single nucleotide polymorphisms, only the naturally occurring D66N (Asp to Asn, GAT to AAT) expanded the binding spectrum to host plant proteins of the heavy metal associated (HMA) family. In contrast, three of the nonsynonymous substitutions were deleterious resulting in loss of binding to HMA proteins. Additionally, we identified three cases of homoplasy in the APikL effector family, involving HMA-binding interfaces, indicating recurrent convergent evolution. Our findings suggest an experimental framework for predicting evolutionary outcomes of pathogen effector--host target interactions with implications for plant disease resistance breeding.
]]></description>
<dc:creator>Langner, T.</dc:creator>
<dc:creator>Maqbool, A.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2025-08-12</dc:date>
<dc:identifier>doi:10.1101/2025.08.12.669671</dc:identifier>
<dc:title><![CDATA[Rewinding the tape: historical contingency and functional constraints have shaped the evolution of APikL virulence effectors in the blast fungus]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-08-12</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.08.16.670655v1?rss=1">
<title>
<![CDATA[
A Phosphorelay Circuit Drives Extracellular Alkalinization in Plant Receptor Kinase Signaling 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.08.16.670655v1?rss=1"
</link>
<description><![CDATA[
Extracellular alkalinization has long been recognized as a hallmark of plant cell-surface receptor activation, including during pattern-triggered immunity (PTI); yet the mechanisms driving elicitor-induced alkalinization and its role in immune signaling remain unclear. Here, we demonstrate that inhibition of autoinhibited H+-ATPases (AHAs) is required for elicitor-induced extracellular alkalinization. This alkalinization is essential for immune signaling mediated by diverse plasma membrane-localized receptor kinases (RKs) through modulation of ligand-receptor interactions. Notably, RKs transduce elicitor-triggered signaling via BOTRYTIS-INDUCED KINASE 1 (BIK1), which inhibits AHA activity by disrupting AHA-GENERAL REGULATORY FACTOR (GRF) interactions through a conserved phosphorylation event. Interestingly, this pathway is crucial for cell wall damage (CWD) responses involving the RK MALE DISCOVERER 1-INTERACTING RECEPTOR LIKE KINASE 2 (MIK2) and its ligand, SERINE RICH ENDOGENOUS PEPTIDE 18 (SCOOP18). Our findings reveal a conserved phospho-regulatory pathway that governs extracellular alkalinization to coordinate plant immune signaling, offering new insights into plant stress resilience.
]]></description>
<dc:creator>Zhai, K.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Zhang, S.</dc:creator>
<dc:creator>Choi, S.</dc:creator>
<dc:creator>Wang, L.</dc:creator>
<dc:creator>Song, B.</dc:creator>
<dc:creator>Kinoshita, T.</dc:creator>
<dc:creator>Zhou, J.-M.</dc:creator>
<dc:creator>Menke, F.</dc:creator>
<dc:creator>Bender, K. W.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2025-08-20</dc:date>
<dc:identifier>doi:10.1101/2025.08.16.670655</dc:identifier>
<dc:title><![CDATA[A Phosphorelay Circuit Drives Extracellular Alkalinization in Plant Receptor Kinase Signaling]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-08-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.08.26.672026v1?rss=1">
<title>
<![CDATA[
An activated wheat CCG10-NLR immune receptor forms an octameric resistosome 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.08.26.672026v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding and leucine-rich repeat (LRR) receptors (NLRs) are widespread intracellular immune sensors across kingdoms. In plants, the G10-type coiled-coil (CCG10)-NLRs form a distinct phylogenetic clade that remains poorly characterized. Here, we identified a gain-of-function (GOF) mutant of Wheat Autoimmunity 3 (WAI3), designated WAI3GOF, which encodes a constitutively activated CCG10-NLR protein due to an amino acid substitution. Cryo-EM structural analysis revealed that activated WAI3 assembles into a distinctive octameric resistosome. Arabidopsis RPS2, another CCG10-NLR, also forms an octamer, indicating a conserved structural property across monocot and dicot plants. The WAI3 resistosome mediates a prolonged and sustained increase in cytosolic calcium influx, facilitated by a unique channel architecture arising from its divergent CC domain configuration. Notably, this domain arrangement may be shared by many plant NLRs that lack the conserved EDVID motif in their CC domains. Our findings uncover a previously uncharacterized resistosome structure and provide insights into plant immune receptor plasticity.
]]></description>
<dc:creator>Guo, G.</dc:creator>
<dc:creator>Zhao, H.</dc:creator>
<dc:creator>Bai, K.</dc:creator>
<dc:creator>Wu, Q.</dc:creator>
<dc:creator>Dong, L.</dc:creator>
<dc:creator>Lu, L.</dc:creator>
<dc:creator>Chen, Y.</dc:creator>
<dc:creator>Hou, Y.</dc:creator>
<dc:creator>Lu, J.</dc:creator>
<dc:creator>Lu, P.</dc:creator>
<dc:creator>Li, M.</dc:creator>
<dc:creator>Zhang, H.</dc:creator>
<dc:creator>Wang, G.</dc:creator>
<dc:creator>Zhu, K.</dc:creator>
<dc:creator>Huang, B.</dc:creator>
<dc:creator>Cui, X.</dc:creator>
<dc:creator>Fu, H.</dc:creator>
<dc:creator>Hu, C.</dc:creator>
<dc:creator>Chu, Z.</dc:creator>
<dc:creator>Lyu, X.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Wang, C.</dc:creator>
<dc:creator>Liu, Z.</dc:creator>
<dc:creator>Selvaraj, M.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:date>2025-08-27</dc:date>
<dc:identifier>doi:10.1101/2025.08.26.672026</dc:identifier>
<dc:title><![CDATA[An activated wheat CCG10-NLR immune receptor forms an octameric resistosome]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-08-27</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.10.06.680644v1?rss=1">
<title>
<![CDATA[
Synchronous spatio-temporal control of autophagy and organelle trafficking is necessary for appressorium-mediated plant infection by Magnaporthe oryzae 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.10.06.680644v1?rss=1"
</link>
<description><![CDATA[
The blast fungus Magnaporthe oryzae infects plants using a specialised infection structure called an appressorium that generates physical force to break the rice leaf cuticle. Appressorium development follows a cell cycle-controlled morphogenetic program, requiring autophagy-associated cell death of the fungal spore from which the infection cell develops. How proliferative growth of the fungus is regulated at the same time as programmed cell death, however, is unknown. In this study, we provide evidence that each cell of the conidium undergoes a separate developmental program, which is necessary for plant infection. Using quantitative live-cell imaging, we monitored trafficking of ten organelle types during appressorium morphogenesis in a wild-type M. oryzae strain and isogenic {Delta}atg8 autophagic mutant. High-resolution microscopy using a photoactivatable green fluorescent protein revealed that organelle trafficking occurs from a single conidium cell into the appressorium, while the remaining two cells undergo autophagy. Organelle inheritance operates independently of cell cycle checkpoints but is always associated with spore germination. We furthermore defined the temporal sequence of organelle movement and de novo organelle biogenesis in the incipient appressorium using photoconvertible fluorescent localisation microscopy. Taken together, our study reveals how synchronous spatiotemporal control of autophagy and organelle trafficking is necessary for rice blast infection.
]]></description>
<dc:creator>Eseola, A. B.</dc:creator>
<dc:creator>Yan, X.</dc:creator>
<dc:creator>Oses-Ruiz, M.</dc:creator>
<dc:creator>Ryder, L. S.</dc:creator>
<dc:creator>Egan, M. J.</dc:creator>
<dc:creator>MacLean, D.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:date>2025-10-06</dc:date>
<dc:identifier>doi:10.1101/2025.10.06.680644</dc:identifier>
<dc:title><![CDATA[Synchronous spatio-temporal control of autophagy and organelle trafficking is necessary for appressorium-mediated plant infection by Magnaporthe oryzae]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-10-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.10.06.680679v1?rss=1">
<title>
<![CDATA[
A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.10.06.680679v1?rss=1"
</link>
<description><![CDATA[
Plants secrete a variety of proteases as a defense response during infection by microbial pathogens. However, the relationship between their catalytic activities and antimicrobial functions remains largely unknown. Particularly, few biologically relevant substrates of these proteases have been identified. Huanglongbing (HLB) has been a major threat to the citrus industry worldwide. The HLB-associated bacterium, Candidatus Liberibacter asiaticus (Las), was previously shown to deploy an inhibitor of papain-like cysteine proteases (PLCPs) to promote disease in citrus. In this study, we identified an outer membrane protein (OMP) of Las, LasOMP1, as a substrate of the citrus PLCP CsRD21a. LasOMP1 is one of the most highly expressed genes in Las. CsRD21a cleaves LasOMP1 and produces cleaved peptide products, which could be detected in vitro and in HLB-diseased citrus plants. We found that CsRD21a targets the N-terminal portion of LasOMP1, potentially at an extracellular loop region. Importantly, transgenic sweet orange overexpressing CsRD21a showed reduced Las titers and delayed disease symptoms, highlighting that engineering this protease is a promising strategy to enhance HLB resistance in citrus. Together, our work reveals a pathogen-derived substrate of plant PLCPs and highlights bacterial OMPs as direct targets of plant defense.

Significance StatementHuanglongbing (HLB) is the most devastating disease of citrus with no resistance having been identified in commercial cultivars. Previous work implicated papain-like cysteine proteases (PLCPs) as an important hub of defense in citrus; however, their precise role in HLB tolerance remained unclear. Here, we identify and characterize an outer membrane protein (OMP) from the HLB-associated bacterium as a substrate of the citrus PLCP RD21a. We demonstrate a specific cleavage of the bacterial OMP by citrus RD21a, which may impair pathogen growth and/or activate plant immunity. Importantly, overexpression of RD21a enhances HLB tolerance in sweet oranges. This work identifies OMPs as substrates of plant PLCPs and provides insights into protease defense functions.
]]></description>
<dc:creator>McClelland, A. J.</dc:creator>
<dc:creator>Hu, B.</dc:creator>
<dc:creator>Xu, Y.</dc:creator>
<dc:creator>Wang, C.</dc:creator>
<dc:creator>Lovelace, A. H.</dc:creator>
<dc:creator>Hawara, E.</dc:creator>
<dc:creator>Wang, Y.</dc:creator>
<dc:creator>Pang, Z.</dc:creator>
<dc:creator>De Francesco, A.</dc:creator>
<dc:creator>Levy, A.</dc:creator>
<dc:creator>Wang, N.</dc:creator>
<dc:creator>van der Hoorn, R.</dc:creator>
<dc:creator>XU, Q.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:date>2025-10-06</dc:date>
<dc:identifier>doi:10.1101/2025.10.06.680679</dc:identifier>
<dc:title><![CDATA[A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-10-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.10.20.683271v1?rss=1">
<title>
<![CDATA[
An elevated environmental temperature impairs accumulation of the pattern recognition receptor FLS2 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.10.20.683271v1?rss=1"
</link>
<description><![CDATA[
Pattern-triggered immunity (PTI) is initiated when plants detect pathogen-associated molecular patterns (PAMPs) through pattern-recognition receptors (PRRs). How moderate increases in temperature affect this plant immune signalling remains unclear. We explored this by using flg22 and the leucine-rich repeat receptor kinase (LRR-RK) FLS2 as a model receptor-ligand system and Ca2+ signaling as a representative PTI output. A pre-treatment at 28 {degrees}C significantly impaired the flg22-induced [Ca2+]cyt influx, leading to a reduced expression of calcium-dependent defence genes, ICS1 and EDS1. This effect correlated with a temperature-dependent reduction in FLS2 abundance. A qualitatively similar inhibition of these responses was observed when membrane fluidity was artificially increased using benzyl alcohol. This suggests that the effect of elevated temperature might act through changes in membrane properties. Artificially restoring FLS2 protein levels rescued flg22-dependent Ca2+ signalling and ICS1 and EDS1 expression in seedlings pre-treated at 28{degrees}C or with benzyl alcohol. Together, these findings indicate that increased membrane fluidity reduces FLS2 protein levels, thereby compromising Ca2+ signalling, and probably other, flg22-indcued responses. This highlights a potential mechanistic link between temperature perception, membrane fluidity, and FLS2-dependent calcium signalling, providing insight into how an increase in global temperatures may compromise plant immune responses in the future.
]]></description>
<dc:creator>Jacobs, B. C. I. C.</dc:creator>
<dc:creator>Knight, M. R.</dc:creator>
<dc:creator>Bender, K. W.</dc:creator>
<dc:creator>Six, E.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:date>2025-10-20</dc:date>
<dc:identifier>doi:10.1101/2025.10.20.683271</dc:identifier>
<dc:title><![CDATA[An elevated environmental temperature impairs accumulation of the pattern recognition receptor FLS2]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-10-20</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.06.14.659724v1?rss=1">
<title>
<![CDATA[
Pathogen effector forms a hexameric phosphatase holoenzyme with host core enzyme to promote disease 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.06.14.659724v1?rss=1"
</link>
<description><![CDATA[
Pathogen effectors play critical roles in pathogenesis by directly manipulating host cellular processes. The Ser/Thr protein phosphatase 2A (PP2A) is commonly targeted by pathogens. Effectors from devastating plant pathogen Phytophthora hijack the PP2A core enzyme in plant hosts, altering the host phosphoproteome. In this study, we present a series of cryo-electron microscopy structures of the Phytophthora effector PSR2 in complex with the host PP2A core enzyme to form a functional holoenzyme. The PSR2-PP2A complex adopts a unique hexameric architecture, driven by PSR2-mediated dimerization of two heterotrimers. This hexamer exhibits greater stability and features a more exposed catalytic pocket compared to the canonical trimeric form of PP2A, likely enhancing its virulence activity. Mutational analyses underscore the importance of this hexameric structure for PSR2s virulence function. These findings provide mechanistic insights into pathogen-mediated manipulation of a key host phosphatase and offer targets for developing disease resistance strategies.
]]></description>
<dc:creator>Wang, J.</dc:creator>
<dc:creator>Li, H.</dc:creator>
<dc:creator>Sun, W.</dc:creator>
<dc:creator>Wang, J.</dc:creator>
<dc:creator>Fang, X.</dc:creator>
<dc:creator>Yang, X.</dc:creator>
<dc:creator>Liu, C.</dc:creator>
<dc:creator>Sheng, G.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:creator>Wang, Y.</dc:creator>
<dc:date>2025-06-18</dc:date>
<dc:identifier>doi:10.1101/2025.06.14.659724</dc:identifier>
<dc:title><![CDATA[Pathogen effector forms a hexameric phosphatase holoenzyme with host core enzyme to promote disease]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-06-18</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.10.22.683861v1?rss=1">
<title>
<![CDATA[
Uncoupling hypersensitive cell death response and disease resistance activated by effector-triggered immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.10.22.683861v1?rss=1"
</link>
<description><![CDATA[
Effector-triggered immunity (ETI) is a major defence strategy in plants and is frequently associated with the hypersensitive response (HR), a localized form of programmed cell death long assumed to be essential for pathogen resistance. However, the causal relationship between HR and effective immunity remains unresolved. We show that the Arabidopsis cbp60g sard1 double mutant exhibits exaggerated ETI-associated HR but only partial resistance to bacterial and oomycete pathogens, thereby genetically uncoupling cell death from disease resistance without pleiotropic defects. Genome-wide transcriptome profiling reveals that the absence of CBP60g and SARD1 disrupts the balance between immune activators and suppressors, including reduced induction of the Nudix hydrolase NUDT7. Overexpression of NUDT7 diminishes but does not abolish the heightened HR phenotype in cbp60g sard1 mutant, indicating that multiple negative regulators act redundantly to restrain immune-associated cell death. These findings demonstrate that HR is not an obligatory determinant of effective resistance and provide mechanistic insight into how plants coordinate transcriptional networks to balance pathogen defence with the containment of host cell death. By refining the relationship between HR and immunity, this work challenges a long-standing paradigm in plant biology and advances our understanding of immune regulation.
]]></description>
<dc:creator>Chhillar, H.</dc:creator>
<dc:creator>Schoonbeek, H.-j.</dc:creator>
<dc:creator>Ngou, B. P. M.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Ding, P.</dc:creator>
<dc:date>2025-10-23</dc:date>
<dc:identifier>doi:10.1101/2025.10.22.683861</dc:identifier>
<dc:title><![CDATA[Uncoupling hypersensitive cell death response and disease resistance activated by effector-triggered immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-10-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.10.24.684422v1?rss=1">
<title>
<![CDATA[
Disulfide bond sculpts a peptide fold that mediates phytocytokine recognition 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.10.24.684422v1?rss=1"
</link>
<description><![CDATA[
Precise ligand recognition by closely related leucine-rich repeat receptor kinases (LRR-RKs) is essential for plants to coordinate immunity, development, and environmental adaptation. Here, we show how HAESA-LIKE 3 (HSL3) specifically recognizes the folded, disulfide-stabilized CTNIP/SCREW phytocytokines in Arabidopsis. Quantitative binding assays define a minimal CTNIP4 region required for high-affinity HSL3 interaction and signaling activation. A 2.12 [A] crystal structure of the HSL3-CTNIP4 complex reveals a unique C-terminal receptor pocket that accommodates the peptides cyclic architecture through a combination of hydrophobic and polar contacts, a feature absent in the closely related HAE/HSL LRR-RKs. The cyclic CTNIP4 fold further establishes a largely hydrophobic interface that bridges HSL3 to the SERK co-receptor, forming a distinct activation surface. Together, these structural, biochemical and physiological insights uncover a previously unrecognised mechanism of peptide perception and receptor activation, highlighting how subtle architectural variations enable precise ligand selectivity among highly conserved plant receptor kinases.
]]></description>
<dc:creator>Jimenez Sandoval, P.</dc:creator>
<dc:creator>Johanndrees, O.</dc:creator>
<dc:creator>Snoeck, S.</dc:creator>
<dc:creator>Harshith, C. Y.</dc:creator>
<dc:creator>Omary, M.</dc:creator>
<dc:creator>Broyart, C.</dc:creator>
<dc:creator>Rhodes, J.</dc:creator>
<dc:creator>Bender, K. W.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Santiago, J.</dc:creator>
<dc:date>2025-10-24</dc:date>
<dc:identifier>doi:10.1101/2025.10.24.684422</dc:identifier>
<dc:title><![CDATA[Disulfide bond sculpts a peptide fold that mediates phytocytokine recognition]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-10-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.10.31.685743v1?rss=1">
<title>
<![CDATA[
Diverse haplotypes at a complex Solanum americanum locus confer resistance to Phytophthora infestans and P. capsici 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.10.31.685743v1?rss=1"
</link>
<description><![CDATA[
Plants encounter diverse pathogens and have evolved a two-layered innate immune system to detect pathogen molecules and activate defense mechanisms that restrict infection. Most cloned plant Resistance (R) genes encode NLR immune receptors. NLR genes are often found in clusters of paralogs with sequence and copy number variation; whether these NLR clusters evolve in response to single or multiple pathogens has been unclear. We report here the isolation of a Phytophthora capsici resistance gene, Rpc2, along with a novel P. infestans resistance gene, Rpi-amr5, from two Solanum americanum accessions. These orthologous genes reside in the Rpi-amr1 cluster, which has previously been associated with resistance to P. infestans. By screening RXLR effector libraries of P. infestans and P. capsici, we identified multiple effectors recognized by both NLRs. Our findings highlight the complexity of NLR clusters and evolution driven by interactions with multiple pathogens. This work will underpin efforts to elevate resistance against Phytophthora pathogens and enhances our understanding of NLR evolution.
]]></description>
<dc:creator>Heal, R.</dc:creator>
<dc:creator>Olave-Achury, A. C.</dc:creator>
<dc:creator>Sindalovskaya, M.</dc:creator>
<dc:creator>Long, L.</dc:creator>
<dc:creator>Karki, H. S.</dc:creator>
<dc:creator>Taylor, J.</dc:creator>
<dc:creator>Wawryk-Khamdavong, A.</dc:creator>
<dc:creator>Bachowska, K.</dc:creator>
<dc:creator>Smoker, M.</dc:creator>
<dc:creator>Alam, M.</dc:creator>
<dc:creator>Pottinger, S.</dc:creator>
<dc:creator>Arora, V.</dc:creator>
<dc:creator>Sohn, K. H.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Lin, X.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:date>2025-10-31</dc:date>
<dc:identifier>doi:10.1101/2025.10.31.685743</dc:identifier>
<dc:title><![CDATA[Diverse haplotypes at a complex Solanum americanum locus confer resistance to Phytophthora infestans and P. capsici]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-10-31</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.11.25.690456v1?rss=1">
<title>
<![CDATA[
Tangerine: a Starship-like element in the genomes of Xanthoria lichen-forming fungi 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.11.25.690456v1?rss=1"
</link>
<description><![CDATA[
Lichens are symbiotic associations between filamentous fungi and photosynthetic micro-organisms, such as algae or cyanobacteria, that result in a single anatomically-complex structure that can thrive in environments inhospitable to most organisms, including arctic tundra, high mountains, and deserts. Recent evidence suggests that lichens may be even more complex than previously appreciated, containing multiple microbial constituents that operate as mini-ecosystems, but how genomes of the principal fungal symbiont (which provides the majority of biomass in lichen tissue) have been shaped during evolution is largely unexplored. Recently, giant transposable elements called Starships have been found in many genomes of filamentous fungi, but to which extent they occur in lichen-forming fungi is not known. In this report, we describe a Starship-like element from the lichen fungus Xanthoria parietina. This element, named Tangerine, contains several genes that have signatures of horizontal gene transfer from non-lichen-forming fungi, most likely from black yeasts of the Chaetothyriales, that are often lichen-associated. Furthermore, the "captain" gene responsible for transposition of the Starship defines a small lichen-specific clade of tyrosine recombinases within clade 1 of the tyrosine recombinase typology, suggesting a longstanding association of these elements with lichen-forming fungi. Internal repeats within Tangerine, and other sites in Xanthoria genomes, are affected by repeat-induced point mutation (RIP), a mechanism of genome defense against transposable elements, consistent with fungal sexual reproduction which always precedes new lichen formation by Xanthoria. We conclude that Starships may have played a significant, yet hitherto unrecognized role, in lichen genome evolution.
]]></description>
<dc:creator>Tagirdzhanova, G.</dc:creator>
<dc:creator>Bucknell, A.</dc:creator>
<dc:creator>Cameron, E. S.</dc:creator>
<dc:creator>Finn, R. D.</dc:creator>
<dc:creator>Blaxter, M.</dc:creator>
<dc:creator>McDonald, M. C.</dc:creator>
<dc:creator>Talbot, N. J.</dc:creator>
<dc:date>2025-11-27</dc:date>
<dc:identifier>doi:10.1101/2025.11.25.690456</dc:identifier>
<dc:title><![CDATA[Tangerine: a Starship-like element in the genomes of Xanthoria lichen-forming fungi]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-11-27</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.12.24.630226v1?rss=1">
<title>
<![CDATA[
Engineering an Exo70 integrated domain of a barley NLR for improved blast resistance 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.12.24.630226v1?rss=1"
</link>
<description><![CDATA[
Intracellular immune receptors protect plants from microbial invasion by detecting and responding to pathogen-derived effector molecules, often triggering cell death responses. However, pathogen effectors can evolve to avoid immune recognition, resulting in devastating diseases that threaten global agriculture. Here, we show that an integrated Exo70 domain from the barley NLR RGH2 can interact with both the rice blast pathogen effector AVR-Pii and a closely related wheat blast variant. We used structure-led engineering to develop RGH2+ that shows increased binding affinity towards AVR-Pii variants and increased cell death responses on heterologous expression in Nicotiana benthamiana. Infection assays in transgenic barley lines carrying RGH2+ with the paired NLR RGH3 indicate a reduced susceptibility to blast strains expressing AVR-Pii variants. These results demonstrate the potential of engineering NLR receptors as an effective strategy for improving resistance towards one of the most destructive diseases affecting cereal production.
]]></description>
<dc:creator>Saado, I.</dc:creator>
<dc:creator>Brabham, H.</dc:creator>
<dc:creator>Bennett, J. W.</dc:creator>
<dc:creator>Lam, A. H. C.</dc:creator>
<dc:creator>Hernandez-Pinzon, I.</dc:creator>
<dc:creator>Moscou, M. J.</dc:creator>
<dc:creator>Concepcion, J. C. D. l.</dc:creator>
<dc:creator>Banfield, M. J.</dc:creator>
<dc:date>2024-12-24</dc:date>
<dc:identifier>doi:10.1101/2024.12.24.630226</dc:identifier>
<dc:title><![CDATA[Engineering an Exo70 integrated domain of a barley NLR for improved blast resistance]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-12-24</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.11.30.691369v1?rss=1">
<title>
<![CDATA[
The Pik NLR pair accumulates at the plasma membrane as a hetero-oligomeric sensor-helper immune protein complex prior to activation 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.11.30.691369v1?rss=1"
</link>
<description><![CDATA[
Following the perception of pathogen virulence proteins in plants, nucleotide-binding and leucine-rich repeat immune receptors (NLRs) are activated via a wide range of mechanisms. Singleton NLRs can both perceive effectors and trigger an immune response, whereas other NLRs specialise in either pathogen recognition (sensor NLRs) or activation of the immune response (helper NLRs). Sensor and helper NLRs can function as genetically linked pairs or in unlinked receptor networks. Although growing evidence suggests that NLRs conditionally oligomerise upon activation, our understanding of the resting state of NLRs prior to effector perception remains limited. Here, we investigated the oligomeric state of the genetically linked rice (Oryza sativa) sensor Pik-1 and helper Pik-2 NLR pair prior to effector activation when transiently expressed in Nicotiana benthamiana leaves. We show that both wild-type Pikm-1 and engineered Pikm-1Enhancer sensors associate with Pikm-2 and form [~]1 MDa hetero-complexes in the resting state that accumulate at the plasma membrane. Our findings contribute to the growing evidence that pre-activation mechanisms vary widely across NLRs. This knowledge could be leveraged for disease resistance engineering strategies complementary to approaches focussing solely on effector binding.

One sentence summaryThe Pik sensor-helper pair of rice immune receptor proteins forms a hetero-oligomer that accumulates at the plasma membrane in its resting state.

SynopsisNucleotide-binding and leucine-rich repeat receptors (NLRs) are key players in plant immune systems that recognise and respond to harmful pathogen effector proteins. NLRs can play specialised roles in either detecting effectors (sensor NLRs) or triggering the immune response (helper NLRs) and might function together as pairs or within larger networks. Although many NLRs are known to oligomerise upon the perception of effectors, much less is understood about their resting state prior to pathogen recognition. In this study, we investigated the resting state of a pair of rice NLRs, Pik-1 and Pik-2, transiently expressed in Nicotiana benthamiana leaves. These two proteins formed a sensor/helper complex at the cell membrane even in the absence of the effector protein. This discovery is significant because it reveals a new aspect of how these immune proteins are organised before activation, contributing to our understanding of the diverse ways plants prepare for immune responses. This finding adds to the growing body of evidence that, although many NLR proteins form complexes to respond to pathogens, their resting states and pre-activation mechanisms can vary widely.
]]></description>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Contreras, M. P.</dc:creator>
<dc:creator>Salguero Linares, J.</dc:creator>
<dc:creator>Luedke, D.</dc:creator>
<dc:creator>Posbeyikian, A.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Marchal, C.</dc:creator>
<dc:date>2025-12-02</dc:date>
<dc:identifier>doi:10.64898/2025.11.30.691369</dc:identifier>
<dc:title><![CDATA[The Pik NLR pair accumulates at the plasma membrane as a hetero-oligomeric sensor-helper immune protein complex prior to activation]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-12-02</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.12.11.693621v1?rss=1">
<title>
<![CDATA[
An embryo-derived peptide signal directs endosperm polarity in Arabidopsis 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.12.11.693621v1?rss=1"
</link>
<description><![CDATA[
Angiosperm seed formation requires the coordinated development of the products of double fertilization, the embryo and the endosperm. The endosperm mediates efficient nutrient transfer from surrounding maternal tissues to the developing embryo. This function requires a polarized tissue organization, which manifests as early polar gene expression and polar cellularization dynamics. We show that the receptor kinase HAIKU2 acts in coordination with the transcription factor WRKY10/MINISEED3 to ensure robust endosperm polarity establishment through the activity of the homeodomain transcription factors WUSCHEL-RELATED HOMEOBOX 8 and 9.

This process depends on egg cell fertilization and is mediated through the peptide PATHOGEN-INDUCED PEPTIDE-LIKE 7, which acts as a HAIKU2 ligand. Our results reveal how a molecular paracrine dialogue between the embryo and endosperm ensures optimal seed developmental coordination.
]]></description>
<dc:creator>Creff, A.</dc:creator>
<dc:creator>Rhodes, J.</dc:creator>
<dc:creator>Salaun, C.</dc:creator>
<dc:creator>Larive, J.</dc:creator>
<dc:creator>Bayle, V.</dc:creator>
<dc:creator>Turley, E.</dc:creator>
<dc:creator>Nobori, T.</dc:creator>
<dc:creator>Figueiredo, D. D.</dc:creator>
<dc:creator>Landrein, B.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Ingram, G.</dc:creator>
<dc:date>2025-12-13</dc:date>
<dc:identifier>doi:10.64898/2025.12.11.693621</dc:identifier>
<dc:title><![CDATA[An embryo-derived peptide signal directs endosperm polarity in Arabidopsis]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-12-13</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.12.19.695480v1?rss=1">
<title>
<![CDATA[
Diploid potato lines for the study and improvement of starch metabolism and structure 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.12.19.695480v1?rss=1"
</link>
<description><![CDATA[
Diploid potato breeding enables faster genetic improvement via selection against deleterious alleles in inbred lines, unlike breeding by intercrossing tetraploid varieties. Starch is the major source of calories in potato tubers, but the starch properties of diploid lines have rarely been reported. In this study, we provide a comprehensive characterisation of tuber and starch properties in two diploid lines that are early isolates from the Solynta breeding program, B26 and B100, and their F1 hybrids. B100 produced fewer, but larger tubers compared to B26, and both diploid lines produced tubers that are smaller than the tetraploid variety, Clearwater Russet. The low tuber yield of B100 correlates with its high self-compatibility and fruit production. Pruning of fruits in B100 significantly increased total tuber yield per plant by stimulating more tuber initiations, but had no effect on average tuber weight, starch content or starch structure. Among the diploid, hybrid and tetraploid lines examined, there were no differences in the total starch content of tubers. Although amylopectin structure and amylose content were similar between the two diploid lines and the tetraploid comparison, B26 had elevated levels of resistant starch and a striking elongated granule morphology. Our results showcase the variation in source-sink relations and starch structure in diploid potato breeding material, demonstrating their potential for research into the genetics underpinning metabolic and quality traits.
]]></description>
<dc:creator>Navarro, T.</dc:creator>
<dc:creator>Dolaptchiev, Y.</dc:creator>
<dc:creator>Bello, O.</dc:creator>
<dc:creator>O'Brien, C.</dc:creator>
<dc:creator>Ortiz, A.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Seung, D.</dc:creator>
<dc:date>2025-12-22</dc:date>
<dc:identifier>doi:10.64898/2025.12.19.695480</dc:identifier>
<dc:title><![CDATA[Diploid potato lines for the study and improvement of starch metabolism and structure]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-12-22</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.12.22.695669v1?rss=1">
<title>
<![CDATA[
An ancient alkalinization factor informs Arabidopsis root development 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.12.22.695669v1?rss=1"
</link>
<description><![CDATA[
The power of hydrogen (pH) regulates virtually all cellular activities. In both plants and animals, cell-to-cell variations in pH correlate with key developmental transitions1-5, yet the underlying regulators and associated functions remain elusive. Here, we report that members of the REMORIN (REM) protein family function as inhibitors of the H+-ATPases thereby promoting extracellular pH (pHe) alkalinization. This, in turn, regulates various cell surface processes, including steroid hormone signaling, and coordinates developmental transitions in the Arabidopsis thaliana root. Inhibition of H+-ATPases by REMs represents an evolutionary innovation that predates the origin of the root system itself. This study thus uncovers an ancient alkalinization mechanism co-opted by the root developmental program and infers that pHe patterning may have shaped morphogenesis evolution.
]]></description>
<dc:creator>Xhelilaj, K.</dc:creator>
<dc:creator>von Arx, M.</dc:creator>
<dc:creator>Biermann, D.</dc:creator>
<dc:creator>Parvanov, A.</dc:creator>
<dc:creator>Faiss, N.</dc:creator>
<dc:creator>Monte, I.</dc:creator>
<dc:creator>Klingelhuber, F.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Timmermans, M.</dc:creator>
<dc:creator>Oecking, C.</dc:creator>
<dc:creator>Gronnier, J.</dc:creator>
<dc:date>2025-12-23</dc:date>
<dc:identifier>doi:10.64898/2025.12.22.695669</dc:identifier>
<dc:title><![CDATA[An ancient alkalinization factor informs Arabidopsis root development]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-12-23</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.12.17.694812v1?rss=1">
<title>
<![CDATA[
Structural basis for heat tolerance in plant NLR immune receptors. 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.12.17.694812v1?rss=1"
</link>
<description><![CDATA[
Nucleotide-binding leucine-rich repeat (NLR) immune receptors sense pathogen molecules and oligomerize, initiating defense signaling. Some NLRs function poorly at elevated temperatures for unknown reasons. We show that temperature-sensitive NLRs retain ligand binding at elevated temperatures but are impaired in oligomerization. We identify key residues involved in temperature resilience. Structural modeling reveals stabilizing intramolecular interactions of the NB-ARC domain with surface residues of the adjacent leucine-rich repeat (LRR) that preserve receptor integrity and functionality under heat stress. These insights enable in silico classification of NLRs as temperature-sensitive or -tolerant and underpin design of temperature tolerant variants of temperature sensitive NLRs.

These findings provide a mechanistic basis for temperature sensitivity in plant immune receptors and enable engineering of temperature-tolerant disease resistance in crops.
]]></description>
<dc:creator>Grech-Baran, M.</dc:creator>
<dc:creator>Witek, K.</dc:creator>
<dc:creator>Ahn, H.-K.</dc:creator>
<dc:creator>Lichocka, M.</dc:creator>
<dc:creator>Vargas-Cortez, T.</dc:creator>
<dc:creator>Barymow-Filoniuk, I.</dc:creator>
<dc:creator>Witek, A. I.</dc:creator>
<dc:creator>Hennig, J.</dc:creator>
<dc:creator>Jones, J. D.</dc:creator>
<dc:creator>Poznanski, J. T.</dc:creator>
<dc:date>2025-12-17</dc:date>
<dc:identifier>doi:10.64898/2025.12.17.694812</dc:identifier>
<dc:title><![CDATA[Structural basis for heat tolerance in plant NLR immune receptors.]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-12-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.12.17.694896v1?rss=1">
<title>
<![CDATA[
Integrating and refining the predictions of ensembled plant effector detection programs using machine learning 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.12.17.694896v1?rss=1"
</link>
<description><![CDATA[
Effectors are pathogen proteins that facilitate infection by manipulating plant immunity. Computational programs have been developed that identify effectors from sequence data. Many of these programs use internal models that have unavoidable biases due to their training processes and the diverse nature of effector sequence, function and phylogeny. Each programs ability to predict effectors across a broad range of plant pathogens is therefore limited. We hypothesised that a meta-predictor constructed using machine learning (ML) approaches could integrate predictions from multiple programs and improve our ability to predict effectors more accurately from bacteria, fungi, and oomycetes. We trained a range of classifiers using classical ML approaches and deep neural networks (DNNs), then selected eight: Random Forest (RF), Support Vector Machine (SVM), Extreme Gradient Boosting (XGBoost), and five DNNs for evaluation. The training, test and validation data were carefully curated from effector and non-effector annotated sequence derived from the training and sample data of six programs: EffectorP 3.0, deepredeff, WideEffHunter, EffectorO, EffectiveT3, T3SEpp. The models were tested against existing programs on a test dataset, and we observed better performance from our models. The best-performing model was a DNN (Model_2) that balanced improved sensitivity with specificity across the three taxa. We observed using SHAP that all the features contributed to the output of Model_2, which might be the reason for its superior performance. The DNN was developed into a package, fimep, to allow easy use of our model.
]]></description>
<dc:creator>Odunlami, L.</dc:creator>
<dc:creator>MacLean, D.</dc:creator>
<dc:date>2025-12-19</dc:date>
<dc:identifier>doi:10.64898/2025.12.17.694896</dc:identifier>
<dc:title><![CDATA[Integrating and refining the predictions of ensembled plant effector detection programs using machine learning]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-12-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2026.01.14.699277v1?rss=1">
<title>
<![CDATA[
AMBER and GOLD: Polycistronic Genes for Betaxanthin Production in Plants 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2026.01.14.699277v1?rss=1"
</link>
<description><![CDATA[
Genetically encoded pigments are powerful visual reporters and creative tools for biology, yet in plants the palette of pigment biosynthesis genes has remained largely limited to red betacyanins encoded by RUBY. Here we develop and characterize three new polycistronic constructs AMBER_v1, AMBER_v2, and GOLD that contain betalain biosynthesis enzymes to produce yellow, fluorescent betaxanthins in plant tissues. These tools expand the palette of publicly available pigmentation genes for use in plant research, education, and floral design.
]]></description>
<dc:creator>Desnoyer, N.</dc:creator>
<dc:creator>Hill, L.</dc:creator>
<dc:creator>Youles, M.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:date>2026-01-14</dc:date>
<dc:identifier>doi:10.64898/2026.01.14.699277</dc:identifier>
<dc:title><![CDATA[AMBER and GOLD: Polycistronic Genes for Betaxanthin Production in Plants]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2026-01-14</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2026.01.25.701577v1?rss=1">
<title>
<![CDATA[
NLR immune receptors can exhibit tissue-specific expression patterns across legume species 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2026.01.25.701577v1?rss=1"
</link>
<description><![CDATA[
Pathogen pressure threatens legume crop productivity worldwide. Nucleotide-binding leucine-rich repeat (NLR) immune receptors serve as crucial plant resistance genes, recognizing pathogens and triggering immunity. However, the extent and patterns of NLR expression in different tissues and organs, notably across evolutionary time, remain largely uncharacterized. To investigate tissue-specificity of NLR expression in the Fabaceae (legumes), we conducted comparative analyses integrating phylogenomics and transcriptomics in root and shoot tissues across different legume species. The NLR repertoires of 28 legumes were grouped into five monophyletic clades: coiled-coil NLR (CC-NLR), Toll/interleukin-1 receptor NLR (TIR-NLR), G10-subclade CC NLR (CCG10-NLR), RESISTANCE TO POWDERY MILDEW 8-like CC NLR (CCR-NLR), and TIR-NB-ARC-like {beta}-propeller WD40/tetratricopeptide repeats (TNPs). Most legume NLRs belonged to CC-NLR and TIR-NLR clades, followed by CCG10-NLR, CCR-NLR, and TNP clades. In seven of these species, comparative analysis of NLR expression in leaves versus roots revealed that over half ([~]57%) of expressed NLR genes showed predominant expression in one tissue: 34% in roots (451/1336), and 23% in leaves (311/1336). We identified 324 root-specific NLRs, 171 leaf-specific NLRs, and 841 non-specific NLRs, with an average tissue specificity per species of 32%. The closely related species grass pea (Lathyrus sativus) and pea (Pisum sativum) were an exception, showing higher levels of leaf-specific rather than root-specific NLR expression. We also identified conserved tissue expression patterns across legume species, resulting in a comprehensive resource describing tissue expression bias, enrichment, and specificity for 113 phylogenetic NLR subclasses. These legume NLR repertoires will support comparative studies between species and inform precision-breeding programs considering tissue expression patterns.
]]></description>
<dc:creator>Marques, R. M.</dc:creator>
<dc:creator>Santos, C.</dc:creator>
<dc:creator>Pai, H.</dc:creator>
<dc:creator>Patto, M. C. V.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Kourelis, J.</dc:creator>
<dc:date>2026-01-26</dc:date>
<dc:identifier>doi:10.64898/2026.01.25.701577</dc:identifier>
<dc:title><![CDATA[NLR immune receptors can exhibit tissue-specific expression patterns across legume species]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2026-01-26</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2026.02.04.703898v1?rss=1">
<title>
<![CDATA[
Structural basis for the broad recognition specificity of an Arabidopsis immune receptor 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2026.02.04.703898v1?rss=1"
</link>
<description><![CDATA[
Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors typically confer resistance through recognition of specific pathogen effectors. The Arabidopsis NLR WRR4A defies this paradigm by recognizing multiple sequence-divergent effectors from Albugo candida, conferring resistance to multiple pathogen races. Despite minimal sequence similarity, these effectors share a conserved N-terminal ferredoxin-like fold. Through cryo-EM structure determination of two WRR4A resistosomes bound to sequence-distinct effectors, combined with AlphaFold modelling, we reveal a shape-based recognition mechanism: WRR4A engages structurally conserved backbone features of the effectors in a mostly side chain-independent manner, enabling recognition of diverse effectors with similar three-dimensional architectures. These insights guided successful engineering of WRR4A to acquire novel recognition specificity. In addition, analysis of the monomeric WRR4A resting state reveals a distinct domain architecture characteristic of C-JID-containing TIR-NLRs and informs their activation mechanism. This work provides insights into NLR-mediated broad-spectrum recognition and the potential for structure-informed engineering of improved crop resistance.
]]></description>
<dc:creator>Zhao, H.</dc:creator>
<dc:creator>Szymansky, C.-M.</dc:creator>
<dc:creator>Lyu, X.</dc:creator>
<dc:creator>Huang, J.</dc:creator>
<dc:creator>Derbyshire, P.</dc:creator>
<dc:creator>Menke, F. L. H.</dc:creator>
<dc:creator>Webster, M. M.</dc:creator>
<dc:creator>Kamoun, S.</dc:creator>
<dc:creator>Selvaraj, M.</dc:creator>
<dc:creator>Jones, J. D. G.</dc:creator>
<dc:date>2026-02-07</dc:date>
<dc:identifier>doi:10.64898/2026.02.04.703898</dc:identifier>
<dc:title><![CDATA[Structural basis for the broad recognition specificity of an Arabidopsis immune receptor]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2026-02-07</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2024.10.01.616128v1?rss=1">
<title>
<![CDATA[
Conservation of an immune homeostasis module in land plants 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2024.10.01.616128v1?rss=1"
</link>
<description><![CDATA[
Calcium-dependent protein kinases (CDPKs) decode cellular calcium transients and play diverse roles in plant growth and stress responses, including immunity. In Arabidopsis thaliana (At, Arabidopsis thereafter), AtCPK28 contributes to immune homeostasis by phosphorylating subgroup IV plant U-box proteins AtPUB22/24/25/26, which target the key immune receptor-like cytoplasmic kinase (RLCK) AtBIK1 for turnover. While this module is conserved in multiple angiosperms, it is unclear if the role of CPK28 in immune homeostasis is conserved more broadly across land plants. Here, we took an evolutionary comparative approach to understand the role of CPK28. We identified a single CPK28 ortholog in the liverwort Marchantia polymorpha, MpCPK28, which exhibits Ca2+-dependent kinase activity that is inhibited by calmodulin in vitro. We identified the subgroup IV plant U-box protein MpPUB20e as a substrate of MpCPK28. MpPUB20e is able to ubiquitinate MpPBLa, the functional ortholog of AtBIK1. We also provide preliminary evidence that MpPBLa undergoes proteasomal degradation in Marchantia, suggesting that optimization of MpPBLa protein accumulation is conserved across land plants. Interestingly, while loss of CPK28 function in multiple angiosperm species results in enhanced immune signaling, we find that Marchantia Mpcpk28 mutant alleles do not display enhanced immune-triggered production of reactive oxygen species or resistance to two pathogens. However, transgenic expression of MpCPK28 was able to restore function in Arabidopsis cpk28-1 mutants, suggesting latent functional conservation of MpCPK28. Furthermore, while AtCPK28-mediated phosphorylation of Thr95/94 on AtPUB25/26 is known to contribute to their activation, we could not observe a functional role for the equivalent residue Thr122 on MpPUB20e. Taken together, our results suggest that post-translational fine-tuning by CPK28 is likely to have refined the  PUB-BIK1 module in the vascular plant lineages.
]]></description>
<dc:creator>Dou, R.</dc:creator>
<dc:creator>El Mahboubi, K.</dc:creator>
<dc:creator>Tanney, C. A. S.</dc:creator>
<dc:creator>Chu, J.</dc:creator>
<dc:creator>Bredow, M.</dc:creator>
<dc:creator>Gallo, M. C. R.</dc:creator>
<dc:creator>Lauressergues, D.</dc:creator>
<dc:creator>Keller, J.</dc:creator>
<dc:creator>Miguel, V. N.</dc:creator>
<dc:creator>DeFalco, T. A.</dc:creator>
<dc:creator>Uhrig, R. G.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Delaux, P.-M.</dc:creator>
<dc:creator>Monaghan, J.</dc:creator>
<dc:date>2024-10-01</dc:date>
<dc:identifier>doi:10.1101/2024.10.01.616128</dc:identifier>
<dc:title><![CDATA[Conservation of an immune homeostasis module in land plants]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2024-10-01</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2026.02.18.706620v1?rss=1">
<title>
<![CDATA[
A specialized ARGONAUTE enables trans-species RNA interference in plant immunity 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2026.02.18.706620v1?rss=1"
</link>
<description><![CDATA[
Trans-species RNA interference (tsRNAi), in which plants produce small RNAs (sRNAs) to silence target genes in pathogens, has emerged as a promising strategy for disease control. However, whether tsRNAi constitutes an endogenous, regulated immune response remains unclear. Here, we show that ARGONAUTE10 (AGO10) plays a critical role in pathogen-induced tsRNAi. Loss of AGO10 in Arabidopsis abolished pathogen gene silencing during infection, leading to hypersusceptibility to oomycete and fungal pathogens. Importantly, AGO10 rapidly responds to pathogen infection through increased protein accumulation and re-location into discrete cytoplasmic condensates, thus promoting the production of trans-species sRNAs at the pathogen infection sites. This immune responsiveness relies on the N terminal intrinsically disordered region (IDR) of AGO10, which is responsible for sensing and responding to immune activation. Specific features in the IDR partitions AGO10 into two deeply diverged subgroups, AGO10a and AGO10b, with the immune responsiveness and defense function evolutionarily conserved in AGO10a but not AGO10b. Together, these findings establish tsRNAi as a bona fide, evolutionarily conserved immune response and position AGO10 as a signal-responsive hub linking pathogen perception to tsRNAi-based defense.
]]></description>
<dc:creator>Wang, M.</dc:creator>
<dc:creator>Yang, C.</dc:creator>
<dc:creator>Yuen, E. L.</dc:creator>
<dc:creator>Fang, X.</dc:creator>
<dc:creator>Qi, F.</dc:creator>
<dc:creator>Yang, S.</dc:creator>
<dc:creator>Koch, B. L.</dc:creator>
<dc:creator>Li, K.</dc:creator>
<dc:creator>Hou, Y.</dc:creator>
<dc:creator>Oh, T.</dc:creator>
<dc:creator>Tang, B.</dc:creator>
<dc:creator>Feng, L.</dc:creator>
<dc:creator>Zhang, X.</dc:creator>
<dc:creator>Bozkurt, T. O.</dc:creator>
<dc:creator>Feng, X.</dc:creator>
<dc:creator>Ma, W.</dc:creator>
<dc:date>2026-02-19</dc:date>
<dc:identifier>doi:10.64898/2026.02.18.706620</dc:identifier>
<dc:title><![CDATA[A specialized ARGONAUTE enables trans-species RNA interference in plant immunity]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2026-02-19</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2026.03.05.708959v1?rss=1">
<title>
<![CDATA[
The Receptor Kinase MEE39/ATHE Mediates Cell Wall Integrity Surveillance During Root Vascular Pathogen Infection 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2026.03.05.708959v1?rss=1"
</link>
<description><![CDATA[
Plant cell wall (CW) integrity signaling enables early detection of microbial invasion, yet the receptors involved and their spatial and temporal dynamics during infection remain largely unknown. We identify ATHENA (ATHE)/MEE39, a previously uncharacterized malectin-like leucin-rich repeat receptor kinase (Mal-LRR-RK) that contributes to defense against the root vascular pathogen Fusarium oxysporum (Fo), particularly in outer root layers where colonization begins. ATHE abundance, localization, and endocytic trafficking are rapidly remodeled during infection, and loss of ATHE compromises basal immunity and early pathogen-induced transcriptional reprogramming. ATHE responds to altered cellulose synthesis, cellulose-derived oligosaccharides, mechanically induced CW perturbations, and the fungal secreted peptide Fo-RALF. In most of these contexts, ATHE acts together with the LRR-RK MIK2, forming a pathogen-strengthened RK complex that fine-tunes root responses to Fo. This represents the first example of a receptor complex visualized subcellularly in vivo during a plant-microbe interaction. Although Brassicaceae-specific, heterologous expression of ATHE enhanced tomato resistance to Fo, highlighting its functional relevance across plant lineages and its potential use for crop engineering. Our work reveals a previously unrecognized strategy by which plants decode microbial threats through dynamic CW-integrity surveillance.
]]></description>
<dc:creator>Montesinos, J. C.</dc:creator>
<dc:creator>Martin-Dacal, M.</dc:creator>
<dc:creator>Huang, H.-Y.</dc:creator>
<dc:creator>Sancho-Andres, G.</dc:creator>
<dc:creator>Rama, F.</dc:creator>
<dc:creator>Carrillo, L.</dc:creator>
<dc:creator>Kashyap, A.</dc:creator>
<dc:creator>Jimenez-Jimenez, A.</dc:creator>
<dc:creator>Gamez-Arjona, F. M.</dc:creator>
<dc:creator>Broyart, C.</dc:creator>
<dc:creator>Yang, H.</dc:creator>
<dc:creator>Coll, N. S.</dc:creator>
<dc:creator>Santiago, J.</dc:creator>
<dc:creator>Zipfel, C.</dc:creator>
<dc:creator>Sanchez-Rodriguez, C.</dc:creator>
<dc:date>2026-03-06</dc:date>
<dc:identifier>doi:10.64898/2026.03.05.708959</dc:identifier>
<dc:title><![CDATA[The Receptor Kinase MEE39/ATHE Mediates Cell Wall Integrity Surveillance During Root Vascular Pathogen Infection]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2026-03-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2026.03.05.709869v1?rss=1">
<title>
<![CDATA[
Plasma membrane nanoscale dynamics of Arabidopsis leucine-rich repeat receptor kinase complexes 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2026.03.05.709869v1?rss=1"
</link>
<description><![CDATA[
Plasma membrane-localized receptors operate as dynamic signaling complexes and integrative networks1-3, yet the spatial and temporal regulation of these interactions remain largely unknown. Here, by analyzing the components of a minimal Arabidopsis leucine-rich repeat receptor kinase network, we describe the differential diffusion and organization of receptor complex components and unveil the nanoscale spatial and temporal logic underlying the formation of receptor kinase complexes. The ligand-binding receptors FLS2 and BRI1, and the accessory receptor BIR3, are organized in plasma membrane nanodomains, within which the co-receptor BAK1 diffuses and is spatially arrested upon ligand perception. BAK1s spatial arrest relies on extracellular domain (ECD)-ECD interactions but does not require receptor complex activation. Mathematical modelling, single molecule imaging and bio-assays infer that accessory receptors maintain a dynamic pool of co-receptors in the vicinity of ligand-binding receptors to promote ligand-induced complex formation and signaling. We propose that ligand-induced receptor kinase complex formation is a deterministic process defined by the relative nanoscale spatial positioning of individual signaling and regulatory components.
]]></description>
<dc:creator>von Arx, M.</dc:creator>
<dc:creator>Jolivet, M.-D.</dc:creator>
<dc:creator>Biermann, D.</dc:creator>
<dc:creator>Gabani, V.</dc:creator>
<dc:creator>Andrews, S. S.</dc:creator>
<dc:creator>Zipfel, C. S.</dc:creator>
<dc:creator>Gronnier, J.</dc:creator>
<dc:date>2026-03-06</dc:date>
<dc:identifier>doi:10.64898/2026.03.05.709869</dc:identifier>
<dc:title><![CDATA[Plasma membrane nanoscale dynamics of Arabidopsis leucine-rich repeat receptor kinase complexes]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2026-03-06</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2025.12.17.694876v1?rss=1">
<title>
<![CDATA[
Stepwise and lineage-specific divergence of a major immune co-chaperone complex in leptosporangiate ferns 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2025.12.17.694876v1?rss=1"
</link>
<description><![CDATA[
Protein-protein interactions are essential for proper cellular function and are often under strong evolutionary pressures to maintain their stability and specificity. In plants, a broadly distributed chaperone complex comprised of the RAR1 (REQUIRED FOR MLA12 RESISTANCE 1) and SGT1 (SUPRESSOR OF THE G2 ALLELE OF SKP1) co-chaperones alongside the HSP90 (HEAT SHOCK PROTEIN90) core chaperone are important for immunity. Despite its importance in flowering plants, a deeper understanding of how this complex evolved remains limited. Here, we examine the molecular evolutionary history of the RAR1-SGT1 interaction across land plants. We identified a lineage-specific divergence of the RAR1-SGT1 binding interface in vascular non-seed ferns, which renders orthologs unable to interact outside of their lineage. Further investigation of interface diversity uncovered a single amino acid residue in RAR1 and three corresponding residues in SGT1 that dictate binding specificity. Ancestral state reconstruction supported stepwise evolution of specificity in SGT1 in leptopsporangiate ferns, which was initiated by a promiscuous intermediate state that widened its capacity to bind RAR1 before subsequent mutations locked in specificity. Our data highlight the broad conservation of the RAR1-SGT1 interface and the coevolutionary dynamics that shaped interface maintenance during lineage-specific diversification.
]]></description>
<dc:creator>Jeong, H.-M.</dc:creator>
<dc:creator>Sugihara, Y.</dc:creator>
<dc:creator>Webster, M. W.</dc:creator>
<dc:creator>Carella, P.</dc:creator>
<dc:date>2025-12-17</dc:date>
<dc:identifier>doi:10.64898/2025.12.17.694876</dc:identifier>
<dc:title><![CDATA[Stepwise and lineage-specific divergence of a major immune co-chaperone complex in leptosporangiate ferns]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2025-12-17</prism:publicationDate>
<prism:section></prism:section>
</item>
<item rdf:about="https://biorxiv.org/cgi/content/short/2026.02.14.705750v1?rss=1">
<title>
<![CDATA[
Transposable Element Diversification and the Evolution of Peltigerales Lichen Symbionts 
]]>
</title>
<link>
https://biorxiv.org/cgi/content/short/2026.02.14.705750v1?rss=1"
</link>
<description><![CDATA[
Lichens are composite organisms formed through the symbiotic association between fungi, algae and/or bacteria. Multiple independent origins of the lichenized lifestyle have been reported in both fungal and algal lineages, but the molecular mechanisms and evolution underpinning these symbiotic relationships remain largely unknown. In this study, we performed long-read metagenomic sequencing on 11 Peltigerales lichen species to characterize the genomic content of lichen symbionts via metagenome assembled genomes (MAGs). Peltigerales genomes generated in this work represent the largest Lecanoromycetes genome sequenced to date, driven by high transposable element content. Transposable elements (TEs) are known to drive genome evolution in other symbioses but have been underexplored in lichen symbionts due technological limitations. Transcriptomics revealed that many genes associated with adaptations to the lichenized lifestyle are associated with TEs suggesting that they may play a key role in the evolution of lichenization.
]]></description>
<dc:creator>Cameron, E. S.</dc:creator>
<dc:creator>Tremblay, B. J.-M.</dc:creator>
<dc:creator>Yahr, R.</dc:creator>
<dc:creator>Blaxter, M.</dc:creator>
<dc:creator>Finn, R. D.</dc:creator>
<dc:date>2026-02-15</dc:date>
<dc:identifier>doi:10.64898/2026.02.14.705750</dc:identifier>
<dc:title><![CDATA[Transposable Element Diversification and the Evolution of Peltigerales Lichen Symbionts]]></dc:title>
<dc:publisher>Cold Spring Harbor Laboratory Press</dc:publisher>
<prism:publicationDate>2026-02-15</prism:publicationDate>
<prism:section></prism:section>
</item>
</rdf:RDF>
