| Literature DB >> 25355893 |
Lauren Turrell1, Edward C Hutchinson1, Frank T Vreede2, Ervin Fodor2.
Abstract
In the influenza virus ribonucleoprotein complex, the oligomerization of the nucleoprotein is mediated by an interaction between the tail-loop of one molecule and the groove of the neighboring molecule. In this study, we show that phosphorylation of a serine residue (S165) within the groove of influenza A virus nucleoprotein inhibits oligomerization and, consequently, ribonucleoprotein activity and viral growth. We propose that nucleoprotein oligomerization in infected cells is regulated by reversible phosphorylation.Entities:
Mesh:
Substances:
Year: 2014 PMID: 25355893 PMCID: PMC4300657 DOI: 10.1128/JVI.02332-14
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103