A Fusarium graminearum effector protein subverts plant immunity by targeting the TaRPM1–TaHSA32 regulatory axis

A Fusarium graminearum effector protein subverts plant immunity by targeting the TaRPM1–TaHSA32 regulatory axis | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article A Fusarium graminearum effector protein subverts plant immunity by targeting the TaRPM1–TaHSA32 regulatory axis Yuan Chen, Qunqing Wang, Yiman Wan, Xiaohui Li, Chunxue Xie, Zhen Wang, and 9 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-8477788/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract Fusarium graminearum is a devastating wheat pathogen that suppresses host immunity to promote infection. Here, we show that the secreted effector FgUP7 contributes to pathogen virulence by targeting the NLR immune receptor TaRPM1. TaRPM1 positively regulates wheat resistance to F. graminearum. By binding the coiled-coil domain, FgUP7 interferes with early NLR oligomerization and promotes TaRPM1 destabilization. In contrast, the heat-induced co-chaperone TaHSA32 associates with TaRPM1 to stabilize the receptor and prime NLR complexes for activation under fluctuating temperatures. Competitive displacement of TaHSA32 by FgUP7 removes this protective layer, rendering TaRPM1 vulnerable to degradation and thereby diminishing host immune surveillance. This antagonistic interplay provides a mechanistic framework explaining how elevated temperature and pathogen effectors synergistically compromise plant immunity. Notably, transgenic manipulation of TaHSA32 or TaRPM1 does not affect major agronomic traits, highlighting the potential for targeted improvement of resistance. Furthermore, the RPM1–HSA32 regulatory axis is functionally conserved in the model grass Brachypodium distachyon, suggesting evolutionary conservation across monocots. Biological sciences/Plant sciences/Plant immunity/Effectors in plant pathology Biological sciences/Plant sciences/Plant immunity/Pattern recognition receptors in plants usarium graminearum wheat NLR immune receptor heat-stress-associated 32-kD protein plant immunity pathogen effector Full Text Additional Declarations There is NO Competing Interest. Supplementary Files SupplementaryFigure.pdf Supplementary Figure SupplementaryInformationfiles.xlsx Supplementary Information Data Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. 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Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-8477788","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":570077663,"identity":"bd2fa7fb-c43e-46bc-9a87-302fcd71c26f","order_by":0,"name":"Yuan 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axis","fulltext":[],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":true,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":true,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"usarium graminearum, wheat, NLR immune receptor, heat-stress-associated 32-kD protein, plant immunity, pathogen effector","lastPublishedDoi":"10.21203/rs.3.rs-8477788/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-8477788/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"Fusarium graminearum is a devastating wheat pathogen that suppresses host immunity to promote infection. Here, we show that the secreted effector FgUP7 contributes to pathogen virulence by targeting the NLR immune receptor TaRPM1. TaRPM1 positively regulates wheat resistance to F. graminearum. By binding the coiled-coil domain, FgUP7 interferes with early NLR oligomerization and promotes TaRPM1 destabilization. In contrast, the heat-induced co-chaperone TaHSA32 associates with TaRPM1 to stabilize the receptor and prime NLR complexes for activation under fluctuating temperatures. Competitive displacement of TaHSA32 by FgUP7 removes this protective layer, rendering TaRPM1 vulnerable to degradation and thereby diminishing host immune surveillance. This antagonistic interplay provides a mechanistic framework explaining how elevated temperature and pathogen effectors synergistically compromise plant immunity. Notably, transgenic manipulation of TaHSA32 or TaRPM1 does not affect major agronomic traits, highlighting the potential for targeted improvement of resistance. Furthermore, the RPM1–HSA32 regulatory axis is functionally conserved in the model grass Brachypodium distachyon, suggesting evolutionary conservation across monocots.","manuscriptTitle":"A Fusarium graminearum effector protein subverts plant immunity by targeting the TaRPM1–TaHSA32 regulatory axis","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2026-01-07 03:44:40","doi":"10.21203/rs.3.rs-8477788/v1","editorialEvents":[{"type":"communityComments","content":0}],"status":"published","journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true}}],"origin":"","ownerIdentity":"4fdf8bcf-6962-4fba-be6a-c57cb4713c88","owner":[],"postedDate":"January 7th, 2026","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"posted","subjectAreas":[{"id":60658871,"name":"Biological sciences/Plant sciences/Plant immunity/Effectors in plant pathology"},{"id":60658872,"name":"Biological sciences/Plant sciences/Plant immunity/Pattern recognition receptors in plants"}],"tags":[],"updatedAt":"2026-01-28T07:00:53+00:00","versionOfRecord":[],"versionCreatedAt":"2026-01-07 03:44:40","video":"","vorDoi":"","vorDoiUrl":"","workflowStages":[]},"version":"v1","identity":"rs-8477788","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-8477788","identity":"rs-8477788","version":["v1"]},"buildId":"XKTyCvWXoU3ODBz1xrDgd","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}