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dc.contributor.authorBattles, Michael B
dc.contributor.authorMas-Lloret, Vicente 
dc.contributor.authorOlmedillas Cela, Eduardo 
dc.contributor.authorCano, Olga 
dc.contributor.authorVazquez-Alcaraz, Monica 
dc.contributor.authorRodriguez, Laura 
dc.contributor.authorMelero, Jose Antonio 
dc.contributor.authorMcLellan, Jason S
dc.date.accessioned2019-02-19T10:27:45Z
dc.date.available2019-02-19T10:27:45Z
dc.date.issued2017-11-16
dc.identifier.citationNat Commun. 2017 Nov 16;8(1):1528.es_ES
dc.identifier.issn2041-1723es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/7181
dc.description.abstractHuman metapneumovirus (hMPV) is a frequent cause of bronchiolitis in young children. Its F glycoprotein mediates virus-cell membrane fusion and is the primary target of neutralizing antibodies. The inability to produce recombinant hMPV F glycoprotein in the metastable pre-fusion conformation has hindered structural and immunological studies. Here, we engineer a pre-fusion-stabilized hMPV F ectodomain and determine its crystal structure to 2.6 Å resolution. This structure reveals molecular determinants of strain-dependent acid-induced fusion, as well as insights into refolding from pre- to post-fusion conformations. A dense glycan shield at the apex of pre-fusion hMPV F suggests that antibodies against this site may not be elicited by host immune responses, which is confirmed by depletion studies of human immunoglobulins and by mouse immunizations. This is a major difference with pre-fusion F from human respiratory syncytial virus (hRSV), and collectively our results should facilitate development of effective hMPV vaccine candidates.es_ES
dc.description.sponsorshipThis work was supported in part by grants 5T32AI007519-18 (M.B.B.), SAF2015-67033-R (J.A.M.), and P20GM113132 (J.S.M.).es_ES
dc.language.isoenges_ES
dc.publisherNature Publishing Group es_ES
dc.type.hasVersionVoRes_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subject.meshAnimals es_ES
dc.subject.meshAntibodies, Neutralizing es_ES
dc.subject.meshAntibodies, Viral es_ES
dc.subject.meshCercopithecus aethiopses_ES
dc.subject.meshCrystallography, X-Ray es_ES
dc.subject.meshFemale es_ES
dc.subject.meshImmunoglobulins, Intravenous es_ES
dc.subject.meshMetapneumovirus es_ES
dc.subject.meshMice es_ES
dc.subject.meshMice, Inbred BALB C es_ES
dc.subject.meshProtein Domains es_ES
dc.subject.meshProtein Engineering es_ES
dc.subject.meshProtein Refolding es_ES
dc.subject.meshRecombinant Proteins es_ES
dc.subject.meshRespiratory Syncytial Virus, Human es_ES
dc.subject.meshVero Cells es_ES
dc.subject.meshViral Fusion Proteins es_ES
dc.titleStructure and immunogenicity of pre-fusion-stabilized human metapneumovirus F glycoproteines_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución 4.0 Internacional*
dc.identifier.pubmedID29142300es_ES
dc.format.volume8es_ES
dc.format.number1es_ES
dc.format.page1528es_ES
dc.identifier.doi10.1038/s41467-017-01708-9es_ES
dc.description.peerreviewedes_ES
dc.relation.publisherversionhttps://doi.org/10.1038/s41467-017-01708-9es_ES
dc.identifier.journalNature communicationses_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/SAF2015-67033-Res_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/P20GM113132es_ES
dc.rights.accessRightsopen accesses_ES


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Atribución 4.0 Internacional
Este Item está sujeto a una licencia Creative Commons: Atribución 4.0 Internacional