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dc.contributor.author | Luque, Daniel | |
dc.contributor.author | Gómez-Blanco, Josué | |
dc.contributor.author | Garriga, Damiá | |
dc.contributor.author | Brilot, Axel F | |
dc.contributor.author | González, José M | |
dc.contributor.author | Havens, Wendy M | |
dc.contributor.author | Carrascosa, José L | |
dc.contributor.author | Trus, Benes L | |
dc.contributor.author | Verdaguer, Nuria | |
dc.contributor.author | Ghabrial, Said A | |
dc.contributor.author | Castón, José R | |
dc.date.accessioned | 2020-05-08T12:34:16Z | |
dc.date.available | 2020-05-08T12:34:16Z | |
dc.date.issued | 2014-05-27 | |
dc.identifier.citation | Proc Natl Acad Sci U S A. 2014 May 27;111(21):7641-6. | es_ES |
dc.identifier.issn | 0027-8424 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/9994 | |
dc.description.abstract | Viruses evolve so rapidly that sequence-based comparison is not suitable for detecting relatedness among distant viruses. Structure-based comparisons suggest that evolution led to a small number of viral classes or lineages that can be grouped by capsid protein (CP) folds. Here, we report that the CP structure of the fungal dsRNA Penicillium chrysogenum virus (PcV) shows the progenitor fold of the dsRNA virus lineage and suggests a relationship between lineages. Cryo-EM structure at near-atomic resolution showed that the 982-aa PcV CP is formed by a repeated α-helical core, indicative of gene duplication despite lack of sequence similarity between the two halves. Superimposition of secondary structure elements identified a single "hotspot" at which variation is introduced by insertion of peptide segments. Structural comparison of PcV and other distantly related dsRNA viruses detected preferential insertion sites at which the complexity of the conserved α-helical core, made up of ancestral structural motifs that have acted as a skeleton, might have increased, leading to evolution of the highly varied current structures. Analyses of structural motifs only apparent after systematic structural comparisons indicated that the hallmark fold preserved in the dsRNA virus lineage shares a long (spinal) α-helix tangential to the capsid surface with the head-tailed phage and herpesvirus viral lineage. | es_ES |
dc.description.sponsorship | We thank N. Grigorieff for continuous technical and intellectual support, stimulating discussions, and critical reading of the manuscript; C. Xu for maintaining the Brandeis EM facility and help with data collection; and C. Mark for editorial assistance. A.F.B. was supported by a grant from the Canadian National Science and Engineering Research Council. The Brandeis EM facility is supported by National Institutes of Health Grant P01 GM62580. This work was supported by Spanish Ministry of Economy and Competitivity Grant BFU 2011-29038 (to J.L.C.), Grant BIO2011-24333 (to N.V.), and Grant BIO BFU2011-25902 (to J.R.C.), and by a grant from the National Institutes of Health Intramural Research Program and the Center for Information Technology (to B.L.T.). | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | National Academy of Sciences | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.subject | 3D cryo-EM | es_ES |
dc.subject | chrysovirus | es_ES |
dc.subject | structural homology | es_ES |
dc.subject | virus evolution | es_ES |
dc.subject.mesh | Amino Acid Sequence | es_ES |
dc.subject.mesh | Capsid Proteins | es_ES |
dc.subject.mesh | Cryoelectron Microscopy | es_ES |
dc.subject.mesh | Molecular Sequence Data | es_ES |
dc.subject.mesh | Penicillium chrysogenum | es_ES |
dc.subject.mesh | Protein Folding | es_ES |
dc.subject.mesh | Protein Structure, Tertiary | es_ES |
dc.subject.mesh | RNA Viruses | es_ES |
dc.subject.mesh | RNA, Double-Stranded | es_ES |
dc.subject.mesh | Sequence Analysis, RNA | es_ES |
dc.subject.mesh | Evolution, Molecular | es_ES |
dc.subject.mesh | Models, Molecular | es_ES |
dc.subject.mesh | Nucleic Acid Conformation | es_ES |
dc.title | Cryo-EM near-atomic structure of a dsRNA fungal virus shows ancient structural motifs preserved in the dsRNA viral lineage | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Atribución-NoComercial-CompartirIgual 4.0 Internacional | * |
dc.identifier.pubmedID | 24821769 | es_ES |
dc.format.volume | 111 | es_ES |
dc.format.number | 21 | es_ES |
dc.format.page | 7641-6 | es_ES |
dc.identifier.doi | 10.1073/pnas.1404330111 | es_ES |
dc.contributor.funder | National Institutes of Health (Estados Unidos) | |
dc.contributor.funder | Instituto de Salud Carlos III | |
dc.description.peerreviewed | Sí | es_ES |
dc.identifier.e-issn | 1091-6490 | es_ES |
dc.relation.publisherversion | https://doi.org/10.1073/pnas.1404330111 | es_ES |
dc.identifier.journal | Proceedings of the National Academy of Sciences of the United States of America | es_ES |
dc.repisalud.centro | ISCIII::Centro Nacional de Microbiología | es_ES |
dc.repisalud.institucion | ISCIII | es_ES |
dc.relation.projectID | info:eu_repo/grantAgreement/ES/P01 GM62580 | es_ES |
dc.relation.projectID | info:eu_repo/grantAgreement/ES/BFU 2011-29038 | es_ES |
dc.relation.projectID | info:eu_repo/grantAgreement/ES/BIO2011-24333 | es_ES |
dc.relation.projectID | info:eu_repo/grantAgreement/ES/BFU2011-25902 | es_ES |
dc.rights.accessRights | open access | es_ES |