The Influenza A Virus NS1 Protein Interacts with the Nucleoprotein of Viral Ribonucleoprotein Complexes
Nicole C. Robb, Geoffrey Chase, Katja Bier, Frank T. Vreede, Pang‐Chui Shaw, Nadia Naffakh, Martin Schwemmle, Ervin Fodor
Abstract
Nicole C. Robb, Geoffrey Chase, Katja Bier, Frank T. Vreede, Pang‐Chui Shaw, Nadia Naffakh, Martin Schwemmle, Ervin Fodor
Abstract
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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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.
Key concepts: Nucleoprotein, Ribonucleoprotein, Biology, Virology, H5N1 genetic structure, Influenza A virus, Virus, Orthomyxoviridae