title: Regulation of influenza A virus nucleoprotein oligomerization by phosphorylation.
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.
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
authors.forename: Lauren
authors.initials: L
authors.lastname: Turrell
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
authors.forename: Edward C
authors.initials: EC
authors.lastname: Hutchinson
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom frank.vreede@path.ox.ac.uk ervin.fodor@path.ox.ac.uk.
authors.forename: Frank T
authors.initials: FT
authors.lastname: Vreede
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom frank.vreede@path.ox.ac.uk ervin.fodor@path.ox.ac.uk.
authors.forename: Ervin
authors.initials: E
authors.lastname: Fodor
mesh_terms: D006801:Humans; D053122:Influenza A Virus, H3N2 Subtype / Q000502:physiology*; D019590:Nucleocapsid Proteins; D010766:Phosphorylation; D055503:Protein Multimerization; D016601:RNA-Binding Proteins / Q000378:metabolism*; D014758:Viral Core Proteins / Q000378:metabolism*; D014779:Virus Replication
chemical_list: C048842:NP protein, Influenza A virus; D019590:Nucleocapsid Proteins; D016601:RNA-Binding Proteins; D014758:Viral Core Proteins