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Spectroscopic Investigation of the Kinetic Mechanism Involved in the Association of Potyviral VPg with the Host Plant Translation Initiation Factor eIF4E

hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorWALTER, Jocelyne
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBARRA, Amandine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorCHARON, Justine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorTAVERT-ROUDET, Genevieve
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorMICHON, Thierry
dc.date.issued2020
dc.identifier.issn1661-6596
dc.description.abstractEnThe infectious cycle of potyviruses requires the formation of a complex between the viral genome-linked protein VPg and the host eukaryotic translation initiation factor 4E, eIF4E. Mutations associated with plant resistance to potyviruses were previously mapped at the eIF4E surface, while on the virus side, mutations leading to plant resistance breaking were identified within the VPg. In the present study, fluorescence spectroscopy was used to probe the contribution of the VPg intrinsically disordered region bearing amino acids determinant of the resistance breaking, to the VPg-eIF4E binding mechanism. Synthetic peptides encompassing the VPg 88-120 central region were found to tightly bind to eIF4E. Fluorescence energy transfer experiments show that, upon binding to eIF4E, the N and C termini of the VPg 88-111 fragment move closer to one another, at a distance compatible with a α-helix folding. When the VPg 112-120 region, which contains amino acids associated with resistance breakdown, is appended to VPg 88-111 , the complex formation with eIF4E switches from a single-step to a two-step kinetic model. This study revisits a recent investigation of the VPg-eIF4E complex by specifying the contribution of the VPg central helix and its appended disordered region to VPg association with eIF4E.
dc.language.isoen
dc.publisherMDPI
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.subjectvirus phytopathogène
dc.subjectSanté des plantes
dc.subjectpathologie végétale
dc.subjectvirologie végétale
dc.subject.enintrinsically disordered protein
dc.subject.eneIF4E
dc.subject.enVPg
dc.subject.enpotyvirus
dc.subject.eninduced folding
dc.subject.enprotein-protein interaction
dc.subject.enpre-steady state kinetics
dc.title.enSpectroscopic Investigation of the Kinetic Mechanism Involved in the Association of Potyviral VPg with the Host Plant Translation Initiation Factor eIF4E
dc.typeArticle de revue
dc.identifier.doi10.3390/ijms21165618
dc.subject.halSciences du Vivant [q-bio]
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie
bordeaux.journalInternational Journal of Molecular Sciences
bordeaux.page5618
bordeaux.volume21
bordeaux.issue16
bordeaux.peerReviewedoui
hal.identifierhal-02914077
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02914077v1
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