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dc.contributor.authorMata, Carlos P
dc.contributor.authorLuque, Daniel 
dc.contributor.authorGómez-Blanco, Josué
dc.contributor.authorRodriguez Martinez, Javier M 
dc.contributor.authorGonzález, José M
dc.contributor.authorSuzuki, Nobuhiro
dc.contributor.authorGhabrial, Said A
dc.contributor.authorCarrascosa, José L
dc.contributor.authorTrus, Benes L
dc.contributor.authorCastón, José R
dc.date.accessioned2018-11-16T12:16:15Z
dc.date.available2018-11-16T12:16:15Z
dc.date.issued2017-12-08
dc.identifier.citationPLoS Pathog. 2017 Dec 8;13(12):e1006755.es_ES
dc.identifier.issn1553-7374es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/6619
dc.description.abstractUnlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-Å-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar α-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface.es_ES
dc.description.sponsorshipThis work was supported by grants from the Spanish Ministry of Economy and Competitivity (BFU2013-43149-R to DL and JMR, BFU2014-54181 to JLC and BFU2014-55475-R to JRC), the Madrid regional government (S2013/MIT-2850 to JLC and S2013/MIT-2807 to JRC), the Japanese Ministry of Education, Culture, Sports, Science, and Technology (KAKENHI 25252011 and 16H06436, 16H06429, and 16K21723 to NS), and the NIH Intramural Research Program, Center for Information Technology (to BLT). The CNB-CSIC Proteomics Facility, which belongs to ProteoRed, PRB2-ISCIII, was supported by “Instituto de Salud Carlos III” (ISCIII) grant PT13/000. CPM was a PhD fellow of the La Caixa Foundation International Fellowship Program (La Caixa/CNB). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.es_ES
dc.language.isoenges_ES
dc.publisherPublic Library of Sciencees_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rights.urihttps://creativecommons.org/publicdomain/zero/1.0/*
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshCapsid es_ES
dc.subject.meshCapsid Proteins es_ES
dc.subject.meshConserved Sequence es_ES
dc.subject.meshCryoelectron Microscopy es_ES
dc.subject.meshEvolution, Moleculares_ES
dc.subject.meshImaging, Three-Dimensionales_ES
dc.subject.meshMutagenesis, Insertional es_ES
dc.subject.meshProtein Conformation, alpha-Helical es_ES
dc.subject.meshProtein Conformation, beta-Strand es_ES
dc.subject.meshProtein Interaction Domains and Motifs es_ES
dc.subject.meshProtein Multimerization es_ES
dc.subject.meshProtein Stability es_ES
dc.subject.meshRNA Viruses es_ES
dc.subject.meshSequence Alignment es_ES
dc.subject.meshStructural Homology, Protein es_ES
dc.subject.meshSurface Properties es_ES
dc.subject.meshVirion es_ES
dc.subject.meshXylariales es_ES
dc.subject.meshModels, Moleculares_ES
dc.titleAcquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruseses_ES
dc.typeArtículoes_ES
dc.rights.licenseCC0 1.0*
dc.identifier.pubmedID29220409es_ES
dc.format.volume13es_ES
dc.format.number12es_ES
dc.format.pagee1006755es_ES
dc.identifier.doi10.1371/journal.ppat.1006755es_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderGobierno de Madrides_ES
dc.contributor.funderJapanese Ministry of Education, Culture, Sports, Science, and Technologyes_ES
dc.contributor.funderNational Institutes of Health (United States)es_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn1553-7374es_ES
dc.identifier.journalPLoS pathogenses_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/BFU2013-43149-Res_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/BFU2014-54181es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/BFU2014-55475-Res_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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