The Structure of a Biologically Active Influenza Virus Ribonucleoprotein Complex

PLoS Pathogens

José M. Valpuesta¹  Juan Ortín²  Rocío Coloma²  Rocío Arranz²  José L. Carrascosa²  Jaime Martín-Benito² 

[1] CIBER de Enfermedades Respiratorias (Instituto de Salud Carlos III), Recinto Hospital Joan March, Bunyola, Mallorca, Spain;Centro Nacional de Biotecnología (CSIC), Campus de Cantoblanco, Madrid, Spain

关键词: Ribonucleoproteins;    Polymerases;    Viral structure;    Atomic structure;    RNA structure;    Electron cryo-microscopy;    Ribonucleases;    Influenza viruses;   

DOI  :  10.1371/journal.ppat.1000491

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

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 Å resolution) with two monomers connected to the polymerase complex (at 18 Å 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.

【 授权许可】

CC BY