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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




Journal article


J Virol

Publication Date





1452 - 1455


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