Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1128/JVI.02332-14

Type

Journal article

Journal

J Virol

Publication Date

15/01/2015

Volume

89

Pages

1452 - 1455

Keywords

Humans, Influenza A Virus, H3N2 Subtype, Phosphorylation, Protein Multimerization, RNA-Binding Proteins, Viral Core Proteins, Virus Replication