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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/87867
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dc.contributor.authorLuque, Danieles_ES
dc.contributor.authorGonzález, José M.es_ES
dc.contributor.authorGómez-Blanco, Josuées_ES
dc.contributor.authorMarabini, Robertoes_ES
dc.contributor.authorChichón, Javieres_ES
dc.contributor.authorMena, Ignacioes_ES
dc.contributor.authorAngulo, Ivánes_ES
dc.contributor.authorCarrascosa, José L.es_ES
dc.contributor.authorVerdaguer, Núriaes_ES
dc.contributor.authorTrus, Benes L.es_ES
dc.contributor.authorBárcena, Juanes_ES
dc.contributor.authorCastón, José R.es_ES
dc.date.accessioned2013-11-29T11:07:19Z-
dc.date.available2013-11-29T11:07:19Z-
dc.date.issued2012-
dc.identifierdoi: 10.1128/JVI.07050-11-
dc.identifierissn: 0022-538X-
dc.identifiere-issn: 1098-5514-
dc.identifier.citationJournal of Virology 86(12): 6470-6480 (2012)es_ES
dc.identifier.urihttp://hdl.handle.net/10261/87867-
dc.descriptionet al.-
dc.description.abstractViruses need only one or a few structural capsid proteins to build an infectious particle. This is possible through the extensive use of symmetry and the conformational polymorphism of the structural proteins. Using virus-like particles (VLP) from rabbit hemorrhagic disease virus (RHDV) as a model, we addressed the basis of calicivirus capsid assembly and their application in vaccine design. The RHDV capsid is based on a T=3 lattice containing 180 identical subunits (VP1). We determined the structure of RHDV VLP to 8.0-Å resolution by three-dimensional cryoelectron microscopy; in addition, we used San Miguel sea lion virus (SMSV) and feline calicivirus (FCV) capsid subunit structures to establish the backbone structure of VP1 by homology modeling and flexible docking analysis. Based on the three-domain VP1 model, several insertion mutants were designed to validate the VP1 pseudoatomic model, and foreign epitopes were placed at the N- or C-terminal end, as well as in an exposed loop on the capsid surface. We selected a set of T and B cell epitopes of various lengths derived from viral and eukaryotic origins. Structural analysis of these chimeric capsids further validates the VP1 model to design new chimeras. Whereas most insertions are well tolerated, VP1 with an FCV capsid protein-neutralizing epitope at the N terminus assembled into mixtures of T=3 and larger T=4 capsids. The calicivirus capsid protein, and perhaps that of many other viruses, thus can encode polymorphism modulators that are not anticipated from the plane sequence, with important implications for understanding virus assembly and evolution. © 2012, American Society for Microbiology.-
dc.description.sponsorshipThis work was supported by grants from the Spanish Ministry of Science and Innovation (BFU2009-09331 to R.M., BFU2008-02328/BMC to J.L.C., BIO2008-02556 to N.V., AGL2010-22200-C02-02 to J.B., and BIO2008-02361 and BFU2011-25902 to J.R.C.), NADIR-UE-228394 (to J.B.), and the NIH Intramural Research Program with support from the Center for Information Technology (to B.L.T.).-
dc.language.isoenges_ES
dc.publisherAmerican Society for Microbiologyes_ES
dc.rightsopenAccess-
dc.titleEpitope insertion at the N-terminal molecular switch of the rabbit hemorrhagic disease virus T=3 capsid protein leads to larger T=4 capsidses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1128/JVI.07050-11-
dc.relation.publisherversionhttp://dx.doi.org/10.1128/JVI.07050-11-
dc.date.updated2013-11-29T11:07:19Z-
dc.description.versionPeer Reviewed-
dc.relation.csicSíes_ES
dc.identifier.pmid22491457-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextopen-
item.openairetypeartículo-
item.fulltextWith Fulltext-
item.languageiso639-1en-
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