Regulation of influenza A virus nucleoprotein oligomerization by phosphorylation

J Virol. 2015 Jan 15;89(2):1452-5. doi: 10.1128/JVI.02332-14. Epub 2014 Oct 29.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Humans
  • Influenza A Virus, H3N2 Subtype / physiology*
  • Nucleocapsid Proteins
  • Phosphorylation
  • Protein Multimerization*
  • RNA-Binding Proteins / metabolism*
  • Viral Core Proteins / metabolism*
  • Virus Replication*

Substances

  • NP protein, Influenza A virus
  • Nucleocapsid Proteins
  • RNA-Binding Proteins
  • Viral Core Proteins