Open AccessComparative analysis of mutational robustness of the intrinsically disordered viral protein VPg and of its interactor eIF4E
Author(s) -
Jocelyne Walter,
Justine Charon,
Yihua Hu,
Joy Lachat,
Thomas Leger,
Guillaume Lafforgue,
Amandine Barra,
Thierry Michon
Publication year - 2019
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0211725
Subject(s) - interactor , eif4e , biology , mutant , robustness (evolution) , intrinsically disordered proteins , computational biology , virus , genetics , translation (biology) , gene , microbiology and biotechnology , messenger rna , biophysics
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.