Published in

American Society for Microbiology, Journal of Virology, 2(89), p. 1452-1455, 2015

DOI: 10.1128/jvi.02332-14

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Regulation of Influenza A Virus Nucleoprotein Oligomerization by Phosphorylation

Journal article published in 2014 by Lauren Turrell, Edward C. Hutchinson, Frank T. Vreede, Ervin Fodor ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.