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dc.contributor.authorColoma, Rocío-
dc.contributor.authorValpuesta, José M.-
dc.contributor.authorArranz, Rocío-
dc.contributor.authorCarrascosa, José L.-
dc.contributor.authorOrtín, Juan-
dc.contributor.authorMartín-Benito, Jaime-
dc.identifier.citationPLoS Pathogens 5(6): e1000491en_US
dc.description10 pages, 8 figures.-- PMID: 19557158 [PubMed].-- PMCID: PMC2695768.en_US
dc.descriptionSupporting information (Suppl. figures S1-S5, video S1) available at: http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1000491#s5-
dc.description.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 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.en_US
dc.description.abstract[Author summary] The influenza viruses cause annual epidemics of respiratory disease and occasional pandemics that constitute a major public-health issue. The recent spillover of avian H5N1 and H1N1 swine influenza viruses to humans poses a serious threat of a new pandemic. These viruses contain a segmented RNA genome, which forms independent ribonucleoprotein particles including the polymerase complex and multiple copies of the nucleoprotein. Each of these ribonucleoprotein particles are replicated and express the encoding virus genes independently in the virus-infected cells. To better understand how these processes take place we have determined the three-dimensional structure of a model ribonucleoprotein particle that only contains 248 nucleotides of virus RNA but is biologically active in vitro and in vivo. The structure shows a circular appearance and includes 9 nucleoprotein monomers, two of which are associated to the polymerase complex. Docking of the available atomic structures of the nucleoprotein and domains of the polymerase complex has permitted us to propose a quasi-atomic model for this ribonucleoprotein particle and some of the predictions of the model have been confirmed experimentally by site-directed mutagenesis and phenotype analysis in vitro and in vivo.en_US
dc.description.sponsorshipThis work was supported by the Spanish Ministry of Education and Science (Ministerio de Educación y Ciencia) (grants BFU2004-491, BFU2007-62382 and BFU2007-60046), European Vigilance Network for the Management of Antiviral Drug Resistance (VIRGIL), the VIRHOST Program financed by Comunidad de Madrid and the FLUPOL strep project (SP5B-CT-2007-044263). R.C. was a fellow from Ministerio de Educación y Ciencia.en_US
dc.format.extent507927 bytes-
dc.publisherPublic Library of Scienceen_US
dc.relation.isversionofPublisher’s version-
dc.subjectInfluenza virusesen_US
dc.subjectRNA genomeen_US
dc.subjectVirus transcription and replicationen_US
dc.subjectRibonucleoprotein particles (RNPs)en_US
dc.subjectThree-dimensional structureen_US
dc.titleThe structure of a biologically active influenza virus ribonucleoprotein complexen_US
dc.description.peerreviewedPeer revieweden_US
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