Mostrar el registro sencillo del documento
Structure, Function, and Antigenicity of the SARS- CoV-2 Spike Glycoprotein
dc.creator | Walls, Alexandra C. | |
dc.creator | Park, Young-Jun | |
dc.creator | Tortorici, M. Alejandra | |
dc.creator | Wall, Abigail | |
dc.creator | McGuire, Andrew T. | |
dc.creator | Veesler, David | |
dc.date.accessioned | 2020-09-11T15:49:19Z | |
dc.date.available | 2020-09-11T15:49:19Z | |
dc.date.created | 2020-04-16 | |
dc.identifier.issn | 1097-4172 | spa |
dc.identifier.other | https://www.cell.com/cell/fulltext/S0092-8674(20)30262-2?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS0092867420302622%3Fshowall%3Dtrue | spa |
dc.identifier.uri | http://hdl.handle.net/20.500.12010/13165 | |
dc.format.extent | 19 páginas | spa |
dc.format.mimetype | application/pdf | spa |
dc.language.iso | eng | spa |
dc.publisher | Cell | spa |
dc.source | reponame:Expeditio Repositorio Institucional UJTL | spa |
dc.source | instname:Universidad de Bogotá Jorge Tadeo Lozano | spa |
dc.subject | spike glycoprotein | spa |
dc.subject | antibodies | spa |
dc.subject | neutralizing antibodies | spa |
dc.subject | viral receptor | spa |
dc.subject | cryo-EM | spa |
dc.title | Structure, Function, and Antigenicity of the SARS- CoV-2 Spike Glycoprotein | spa |
dc.type.local | Artículo | spa |
dc.subject.lemb | Síndrome respiratorio agudo grave | spa |
dc.subject.lemb | COVID-19 | spa |
dc.subject.lemb | SARS-CoV-2 | spa |
dc.subject.lemb | Coronavirus | spa |
dc.rights.accessrights | info:eu-repo/semantics/restrictedAccess | spa |
dc.type.hasversion | info:eu-repo/semantics/acceptedVersion | spa |
dc.rights.local | Acceso restringido | spa |
dc.identifier.doi | https://doi.org/10.1016/j.cell.2020.02.058 | spa |
dc.description.abstractenglish | The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination. | spa |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | spa |