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dc.contributor.authorGupta, Yogesh
dc.contributor.authorDagdas, Yasin
dc.contributor.authorMartinez-Rocha, A-L
dc.contributor.authorKershaw, MJ
dc.contributor.authorLittlejohn, George
dc.contributor.authorRyder, Lauren
dc.contributor.authorSklenar, Jan
dc.contributor.authorDelgado Rodriguez, Elena krisstell
dc.contributor.authorNicholas, Talbot
dc.date.accessioned2017-05-24T19:07:22Z
dc.date.available2017-05-24T19:07:22Z
dc.date.issued2015-11
dc.identifier.issn1040-4651
dc.identifier.issn1532-298X
dc.identifier.urihttp://hdl.handle.net/10026.1/9337
dc.description.abstract

Magnaporthe oryzae is the causal agent of rice blast disease, the most devastating disease of cultivated rice (Oryza sativa) and a continuing threat to global food security. To cause disease, the fungus elaborates a specialized infection cell called an appressorium, which breaches the cuticle of the rice leaf, allowing the fungus entry to plant tissue. Here, we show that the exocyst complex localizes to the tips of growing hyphae during vegetative growth, ahead of the Spitzenkörper, and is required for polarized exocytosis. However, during infection-related development, the exocyst specifically assembles in the appressorium at the point of plant infection. The exocyst components Sec3, Sec5, Sec6, Sec8, and Sec15, and exocyst complex proteins Exo70 and Exo84 localize specifically in a ring formation at the appressorium pore. Targeted gene deletion, or conditional mutation, of genes encoding exocyst components leads to impaired plant infection. We demonstrate that organization of the exocyst complex at the appressorium pore is a septin-dependent process, which also requires regulated synthesis of reactive oxygen species by the NoxR-dependent Nox2 NADPH oxidase complex. We conclude that septin-mediated assembly of the exocyst is necessary for appressorium repolarization and host cell invasion.

dc.format.extent3277-3289
dc.format.mediumPrint-Electronic
dc.languageen
dc.language.isoeng
dc.publisherOxford University Press (OUP)
dc.subjectFungal Proteins
dc.subjectHyphae
dc.subjectImmunoprecipitation
dc.subjectMagnaporthe
dc.subjectPlant Diseases
dc.subjectProtein Subunits
dc.subjectProtein Transport
dc.subjectReactive Oxygen Species
dc.subjectSeptins
dc.subjectSpores, Fungal
dc.subjectSubcellular Fractions
dc.titleSeptin-Dependent Assembly of the Exocyst Is Essential for Plant Infection by <i>Magnaporthe oryzae</i>
dc.typejournal-article
dc.typeJournal Article
dc.typeResearch Support, Non-U.S. Gov't
plymouth.author-urlhttps://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000368295800019&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=11bb513d99f797142bcfeffcc58ea008
plymouth.issue11
plymouth.volume27
plymouth.publication-statusPublished
plymouth.journalThe Plant Cell
dc.identifier.doi10.1105/tpc.15.00552
plymouth.organisational-group/Plymouth
plymouth.organisational-group/Plymouth/Faculty of Science and Engineering
plymouth.organisational-group/Plymouth/Faculty of Science and Engineering/School of Biological and Marine Sciences
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA06 Agriculture, Veterinary and Food Science
plymouth.organisational-group/Plymouth/Users by role
plymouth.organisational-group/Plymouth/Users by role/Academics
dc.publisher.placeEngland
dcterms.dateAccepted2015-10-20
dc.identifier.eissn1532-298X
dc.rights.embargoperiodNo embargo
rioxxterms.versionofrecord10.1105/tpc.15.00552
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2015-11
rioxxterms.typeJournal Article/Review


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