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hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorCHARON, Justine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBARRA, Amandine
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorWALTER, Jocelyne
hal.structure.identifierUnité de Pathologie Végétale [PV]
dc.contributor.authorMILLOT, Pauline
hal.structure.identifierUMR - Interactions Plantes Microorganismes Environnement [UMR IPME]
dc.contributor.authorHÉBRARD, Eugénie
hal.structure.identifierUnité de Pathologie Végétale [PV]
dc.contributor.authorMOURY, Benoît
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorMICHON, Thierry
dc.date.issued2018
dc.identifier.issn0737-4038
dc.description.abstractEnIntrinsic disorder (ID) in proteins is defined as a lack of stable structure in physiological conditions. Intrinsically disordered regions (IDRs) are highly abundant in some RNA virus proteomes. Low topological constraints exerted on IDRs are expected to buffer the effect of numerous deleterious mutations and could be related to the remarkable adaptive potential of RNA viruses to overcome resistance of their host. To experimentally test this hypothesis in a natural pathosystem, a set of four variants of Potato virus Y (PVY; Potyvirus genus) containing various ID degrees in the Viral genome-linked (VPg) protein, a key determinant of potyvirus adaptation, was designed. To estimate the ID contribution to the VPg-based PVY adaptation, the adaptive ability of the four PVY variants was monitored in the pepper host (<em>Capsicum annuum</em>) carrying a recessive resistance gene. Intriguingly, the two mutants with the highest ID content displayed a significantly higher ability to restore infection in the resistant host, whereas the less intrinsically disordered mutant was unable to restore infection. The role of ID on virus adaptation may be due either to a larger exploration of evolutionary pathways or the minimization of fitness penalty caused by resistance-breaking mutations. This pioneering study strongly suggests the positive impact of ID in an RNA virus adaptive capacity.
dc.language.isoen
dc.publisherOxford University Press (OUP)
dc.subjectprotein intrinsic disorder
dc.subject.enpotyvirus
dc.subject.enRNA virus adaptation
dc.subject.enresistance breakdown
dc.subject.enviral protein genome-linked
dc.subject.eneukaryotic translation initiation factor 4E
dc.title.enFirst experimental assessment of protein intrinsic disorder involvement in an RNA virus natural adaptive process.
dc.typeArticle de revue
dc.identifier.doi10.1093/molbev/msx249
dc.subject.halSciences du Vivant [q-bio]
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologie/Virologie
bordeaux.journalMolecular Biology and Evolution
bordeaux.page38-49
bordeaux.volume35
bordeaux.issue1
bordeaux.peerReviewedoui
hal.identifierhal-01614825
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01614825v1
bordeaux.COinSctx_ver=Z39.88-2004&amp;rft_val_fmt=info:ofi/fmt:kev:mtx:journal&amp;rft.jtitle=Molecular%20Biology%20and%20Evolution&amp;rft.date=2018&amp;rft.volume=35&amp;rft.issue=1&amp;rft.spage=38-49&amp;rft.epage=38-49&amp;rft.eissn=0737-4038&amp;rft.issn=0737-4038&amp;rft.au=CHARON,%20Justine&amp;BARRA,%20Amandine&amp;WALTER,%20Jocelyne&amp;MILLOT,%20Pauline&amp;H%C3%89BRARD,%20Eug%C3%A9nie&amp;rft.genre=article


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