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dc.contributor.author | Battles, Michael B | |
dc.contributor.author | Mas-Lloret, Vicente | |
dc.contributor.author | Olmedillas Cela, Eduardo | |
dc.contributor.author | Cano, Olga | |
dc.contributor.author | Vazquez-Alcaraz, Monica | |
dc.contributor.author | Rodriguez, Laura | |
dc.contributor.author | Melero, Jose Antonio | |
dc.contributor.author | McLellan, Jason S | |
dc.date.accessioned | 2019-02-19T10:27:45Z | |
dc.date.available | 2019-02-19T10:27:45Z | |
dc.date.issued | 2017-11-16 | |
dc.identifier.citation | Nat Commun. 2017 Nov 16;8(1):1528. | es_ES |
dc.identifier.issn | 2041-1723 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/7181 | |
dc.description.abstract | Human 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.sponsorship | This 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.iso | eng | es_ES |
dc.publisher | Nature Publishing Group | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject.mesh | Animals | es_ES |
dc.subject.mesh | Antibodies, Neutralizing | es_ES |
dc.subject.mesh | Antibodies, Viral | es_ES |
dc.subject.mesh | Cercopithecus aethiops | es_ES |
dc.subject.mesh | Crystallography, X-Ray | es_ES |
dc.subject.mesh | Female | es_ES |
dc.subject.mesh | Immunoglobulins, Intravenous | es_ES |
dc.subject.mesh | Metapneumovirus | es_ES |
dc.subject.mesh | Mice | es_ES |
dc.subject.mesh | Mice, Inbred BALB C | es_ES |
dc.subject.mesh | Protein Domains | es_ES |
dc.subject.mesh | Protein Engineering | es_ES |
dc.subject.mesh | Protein Refolding | es_ES |
dc.subject.mesh | Recombinant Proteins | es_ES |
dc.subject.mesh | Respiratory Syncytial Virus, Human | es_ES |
dc.subject.mesh | Vero Cells | es_ES |
dc.subject.mesh | Viral Fusion Proteins | es_ES |
dc.title | Structure and immunogenicity of pre-fusion-stabilized human metapneumovirus F glycoprotein | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Atribución 4.0 Internacional | * |
dc.identifier.pubmedID | 29142300 | es_ES |
dc.format.volume | 8 | es_ES |
dc.format.number | 1 | es_ES |
dc.format.page | 1528 | es_ES |
dc.identifier.doi | 10.1038/s41467-017-01708-9 | es_ES |
dc.description.peerreviewed | Sí | es_ES |
dc.relation.publisherversion | https://doi.org/10.1038/s41467-017-01708-9 | es_ES |
dc.identifier.journal | Nature communications | 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/SAF2015-67033-R | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/ES/P20GM113132 | es_ES |
dc.rights.accessRights | open access | es_ES |