ArticlePloS one2019
Comparative analysis of mutational robustness of the intrinsically disordered viral protein VPg and of its interactor eIF4E.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- NEDAMSS syndrome-related truncating and missense mutations are associated with aberrant liquid-liquid phase separation of IRF2BPL.Nature communications · 2026Article
- Structural characterization of plum pox virus by cryo-electron microscopy.Archives of virology · 2025Article
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- Evolution of intrinsic disorder in the structural domains of viral and cellular proteomes.Scientific reports · 2025Article
- Analysis of the Contribution of Intrinsic Disorder in Shaping Potyvirus Genetic Diversity.Viruses · 2022Article
- Global genetic diversity and evolutionary patterns amongFrontiers in microbiology · 2022Article
- CRISPR-Cas9 Targeting of theFrontiers in microbiology · 2022Article
- Tuning intrinsic disorder predictors for virus proteins.Virus evolution · 2021Article
- Evolutionary Forces and Codon Bias in Different Flavors of Intrinsic Disorder in the Human Proteome.Journal of molecular evolution · 2020Article
- Article
- New technologies to analyse protein function: an intrinsic disorder perspective.F1000Research · 2020Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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