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Cellular mRNA Export Factor UAP56 Recognizes Nucleic Acid Binding Site of Influenza Virus NP Protein

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Cellular mRNA Export Factor UAP56 Recognizes Nucleic Acid Binding Site of Influenza Virus NP Protein

Andrew K Morris et al. Biochem Biophys Res Commun.

Abstract

Influenza A virus nucleoprotein (NP) is a structural component that encapsulates the viral genome into the form of ribonucleoprotein complexes (vRNPs). Efficient assembly of vRNPs is critical for the virus life cycle. The assembly route from RNA-free NP to the NP-RNA polymer in vRNPs has been suggested to require a cellular factor UAP56, but the mechanism is poorly understood. Here, we characterized the interaction between NP and UAP56 using recombinant proteins and showed that UAP56 features two NP binding sites. In addition to the UAP56 core comprised of two RecA domains, we identified the N-terminal extension (NTE) of UAP56 as a previously unknown NP binding site. In particular, UAP56-NTE recognizes the nucleic acid binding region of NP. This corroborates our observation that binding of UAP56-NTE and RNA to NP is mutually exclusive. Collectively, our results reveal the molecular basis for how UAP56 acts on RNA-free NP, and provide new insights into NP-mediated influenza genome packaging.

Keywords: DEAD-Box ATPase; Host-pathogen interaction; Influenza A virus; RNA-Binding protein; mRNA nuclear export.

Conflict of interest statement

Declaration of competing interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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