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TitleThe structure of a biologically active influenza virus ribonucleoprotein complex.
Journal, issue, pagesPLoS Pathog, Vol. 5, Issue 6, Page e1000491, Year 2009
Publish dateJun 26, 2009
AuthorsRocío Coloma / José M Valpuesta / Rocío Arranz / José L Carrascosa / Juan Ortín / Jaime Martín-Benito /
PubMed AbstractThe influenza viruses contain a segmented, single-stranded RNA genome of negative polarity. Each RNA segment is encapsidated by the nucleoprotein and the polymerase complex into ribonucleoprotein ...The influenza viruses contain a segmented, single-stranded RNA genome of negative polarity. Each RNA segment is encapsidated by the nucleoprotein and the polymerase complex into ribonucleoprotein particles (RNPs), which are responsible for virus transcription and replication. Despite their importance, information about the structure of these RNPs is scarce. We have determined the three-dimensional structure of a biologically active recombinant RNP by cryo-electron microscopy. The structure shows a nonameric nucleoprotein ring (at 12 Angstrom resolution) with two monomers connected to the polymerase complex (at 18 Angstrom resolution). Docking the atomic structures of the nucleoprotein and polymerase domains, as well as mutational analyses, has allowed us to define the interactions between the functional elements of the RNP and to propose the location of the viral RNA. Our results provide the first model for a functional negative-stranded RNA virus ribonucleoprotein complex. The structure reported here will serve as a framework to generate a quasi-atomic model of the molecular machine responsible for viral RNA synthesis and to test new models for virus RNA replication and transcription.
External linksPLoS Pathog / PubMed:19557158 / PubMed Central
MethodsEM (single particle)
Resolution12.0 Å
Structure data

EMDB-1603: 12 Angstrom resolution cryo-electron microscopy reconstruction of a recombinant active ribonucleoprotein particle of influenza virus (9-fold symmetrized).
PDB-2wfs: Fitting of influenza virus NP structure into the 9-fold symmetryzed cryoEM reconstruction of an active RNP particle.
Method: EM (single particle) / Resolution: 12.0 Å

Source
  • Influenza A virus (A/Victoria/3/1975(H3N2))
  • influenza a virus
KeywordsVIRAL PROTEIN / VIRAL NUCLEOPROTEIN / HOST-VIRUS INTERACTION / RNA VIRUSES / NUCLEOPROTEIN / RIBONUCLEOPROTEIN / RNA / VIRION / NUCLEUS / INFLUENZA / RNA-BINDING

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