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The influenza A virus genome consists of eight RNA segments that associate with the viral polymerase proteins (PB1, PB2, and PA) and nucleoprotein (NP) to form ribonucleoprotein complexes (RNPs). The viral NS1 protein was previously shown to associate with these complexes, although it was not clear which RNP component mediated the interaction. Using individual TAP (tandem affinity purification)-tagged PB1, PB2, PA, and NP, we demonstrated that the NS1 protein interacts specifically with NP and not the polymerase subunits. The region of NS1 that binds NP was mapped to the RNA-binding domain.

Original publication

DOI

10.1128/JVI.02562-10

Type

Journal article

Journal

J Virol

Publication Date

05/2011

Volume

85

Pages

5228 - 5231

Keywords

Amino Acid Sequence, Binding Sites, Cell Line, Humans, Molecular Sequence Data, Protein Interaction Mapping, RNA-Binding Proteins, Viral Core Proteins, Viral Nonstructural Proteins