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Comparative analysis of mutational robustness of the intrinsically disordered viral protein VPg and of its interactor eIF4E.

hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorWALTER, Jocelyne
hal.structure.identifierBiologie du fruit et pathologie [BFP]
hal.structure.identifierUniversity of Sydney
dc.contributor.authorCHARON, Justine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorHU, Yihua
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorLACHAT, Joy
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorLEGER, Thomas
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorLAFFORGUE, Guillaume
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBARRA, Amandine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorMICHON, Thierry
dc.date.issued2019
dc.identifier.issn1932-6203
dc.description.abstractEnConformational intrinsic disorder is a feature present in many virus proteins. Intrinsically disordered regions (IDRs) have weaker structural requirement than ordered regions and mutations in IDRs could have a lower impact on the virus fitness. This could favor its exploration of adaptive solutions. The potyviral protein VPg contains IDRs with determinants for adaptation to its host plant. To experimentally assess whether IDRs are more resistant to mutations than ordered regions, the biologically relevant interaction between mutant libraries of both VPg and the eukaryotic translation initiation factor 4E (eIF4E) and their respective wild type partner was examined using yeast two hybrid assay. Our data shows that VPg is significantly more robust to mutations than eIF4E and as such belongs to a particular class of intrinsically disordered proteins. This result is discussed from the standpoint of IDRs involvement in the virus adaptive processes.
dc.language.isoen
dc.publisherPublic Library of Science
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.title.enComparative analysis of mutational robustness of the intrinsically disordered viral protein VPg and of its interactor eIF4E.
dc.typeArticle de revue
dc.identifier.doi10.1371/journal.pone.0211725
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologie/Virologie
bordeaux.journalPLoS ONE
bordeaux.pagee0211725
bordeaux.volume14
bordeaux.issue2
bordeaux.peerReviewedoui
hal.identifierhal-02628650
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02628650v1
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