First experimental assessment of protein intrinsic disorder involvement in an RNA virus natural adaptive process.
hal.structure.identifier | Biologie du fruit et pathologie [BFP] | |
dc.contributor.author | CHARON, Justine | |
hal.structure.identifier | Biologie du fruit et pathologie [BFP] | |
dc.contributor.author | BARRA, Amandine | |
hal.structure.identifier | Génomique, développement et pouvoir pathogène [GD2P] | |
dc.contributor.author | WALTER, Jocelyne | |
hal.structure.identifier | Unité de Pathologie Végétale [PV] | |
dc.contributor.author | MILLOT, Pauline | |
hal.structure.identifier | UMR - Interactions Plantes Microorganismes Environnement [UMR IPME] | |
dc.contributor.author | HÉBRARD, Eugénie | |
hal.structure.identifier | Unité de Pathologie Végétale [PV] | |
dc.contributor.author | MOURY, Benoît | |
hal.structure.identifier | Génomique, développement et pouvoir pathogène [GD2P] | |
dc.contributor.author | MICHON, Thierry | |
dc.date.issued | 2018 | |
dc.identifier.issn | 0737-4038 | |
dc.description.abstractEn | Intrinsic 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.iso | en | |
dc.publisher | Oxford University Press (OUP) | |
dc.subject | protein intrinsic disorder | |
dc.subject.en | potyvirus | |
dc.subject.en | RNA virus adaptation | |
dc.subject.en | resistance breakdown | |
dc.subject.en | viral protein genome-linked | |
dc.subject.en | eukaryotic translation initiation factor 4E | |
dc.title.en | First experimental assessment of protein intrinsic disorder involvement in an RNA virus natural adaptive process. | |
dc.type | Article de revue | |
dc.identifier.doi | 10.1093/molbev/msx249 | |
dc.subject.hal | Sciences du Vivant [q-bio] | |
dc.subject.hal | Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM] | |
dc.subject.hal | Sciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie | |
dc.subject.hal | Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Virologie | |
bordeaux.journal | Molecular Biology and Evolution | |
bordeaux.page | 38-49 | |
bordeaux.volume | 35 | |
bordeaux.issue | 1 | |
bordeaux.peerReviewed | oui | |
hal.identifier | hal-01614825 | |
hal.version | 1 | |
hal.popular | non | |
hal.audience | Internationale | |
hal.origin.link | https://hal.archives-ouvertes.fr//hal-01614825v1 | |
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