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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/993| Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein | |
| Walls, A Park, Y Tortorici, M Wall, A McGuire, A Veesler, D | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| 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-2S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2S 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-2S 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. Wedetermined cryo-EM structures of the SARS-CoV-2S 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. | |
| Cell | |
| 2020 | |
| Preimpreso | |
| https://coronavirus.1science.com/item/88289923c4ac89957a74f138ebaf19dbcd04d4e9 | |
| Inglés | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Artículos científicos |
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