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Turrell, Lauren; Hutchinson, Edward C; Vreede, Frank T; Fodor, Ervin
Journal of virology, 2015-Jan-15, Volume: 89, Issue: 2Journal Article
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.
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