Journal of Virology · 2011 · 60 citations · 27 references
Life SciencesBiochemistryMolecular BiologyMolecular VirologyProtein-protein InteractionsVirologyProtein Complex AssemblyRna StructureRna-binding ProteinsRna-protein InteractionsViral Rna BiologyViral StructureAffinity PurificationNucleic Acid Affinity PurificationProtein-rna Complex StructureRna Virus BiologyRna-binding DomainsRna-protein BindingViral PolymerasesViral Rna-protein Interactions
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.
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