WALTER, Jocelyne; CHARON, Justine; HU, Yihua; LACHAT, Joy; LEGER, Thomas; LAFFORGUE, Guillaume; BARRA, Amandine; MICHON, Thierry

doi:10.1371/journal.pone.0211725

Métadonnées

Afficher la notice complète

Licence d’utilisation du document

WALTER, Jocelyne
Biologie du fruit et pathologie [BFP]

CHARON, Justine
Biologie du fruit et pathologie [BFP]
University of Sydney

HU, Yihua
Biologie du fruit et pathologie [BFP]

Langue

Article de revue

Ce document a été publié dans

PLoS ONE. 2019, vol. 14, n° 2, p. e0211725

Public Library of Science

Résumé en anglais

Conformational 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.< Réduire

Métadonnées

Licence d’utilisation du document

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

Langue

Ce document a été publié dans

Résumé en anglais

DOI

Origine

Unités de recherche