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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/1365| Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion | |
| Walls, A Xiong, X Park, Y Tortorici, M Snijder, J Quispe, J Cameroni, E Gopal, R Dai, M Lanzavecchia, A Zambon, M Rey, F Corti, D Veesler, D | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry intohost cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism. | |
| Cell | |
| 2019 | |
| Preimpreso | |
| https://coronavirus.1science.com/item/43c1bf694fb87a45bfff99dbe3c1b5de0a4f4ba1 | |
| Inglés | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Artículos científicos |
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| 108201.pdf | 9.56 MB | Adobe PDF | Visualizar/Abrir |