Identification of a Novel Complex between the Nucleoprotein and PA(1–27) of Influenza A Virus Polymerase

• DOI: 10.1021/acs.biochem.6b00514
• Publication Date: 2016-07-19T11:53:43Z
• Authors: Jasmina Vidic; Magali Noiray; Angshuman Bagchi; Anny Slama-Schwok
• Keywords: Models, Molecular; 0301 basic medicine; 570; [SDV]Life Sciences [q-bio]; Viral Core Proteins; RNA-Binding Proteins; Molecular Dynamics Simulation; Nucleocapsid Proteins; Surface Plasmon Resonance; RNA-Dependent RNA Polymerase; Recombinant Proteins; Madin Darby Canine Kidney Cells; 3. Good health; Protein Subunits; Viral Proteins; 03 medical and health sciences; Dogs; Influenza A Virus, H1N1 Subtype; Spectrometry, Fluorescence; Multiprotein Complexes; Animals; Protein Interaction Domains and Motifs

The structure of the ribonucleoprotein complexes is crucial to viral transcription and replication of influenza virus, but association of the nucleoprotein (NP) with the polymerase remains to be characterized at the molecular level. Here, we identify a peptide of the polymerase acidic subunit PA(1-27) that associates with NP. Docking and molecular dynamics simulations suggest a similar NP binding site with PA(1-27) and PA(1-186). The PA(1-27)-NP complex is characterized by surface plasmon resonance and fluorescence using recombinant NP proteins and by pull-down assays in infected cells. The PA(1-27)-NP complex may have a role in the final steps of transcription and replication.