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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/4669| A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV | |
| Meng Yuan. Nicholas C. Wu. Xueyong Zhu. Chang-Chun D. Lee. Ray T. Y. So. Huibin Lv. Chris K. P. Mok. Ian A. Wilson. | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| 10.1101/2020.03.13.991570 | |
| The outbreak of COVID-19, which is caused by SARS-CoV-2 virus, continues to spread globally, but there is currently very little understanding of the epitopes on the virus. In this study, we have determined the crystal structure of the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein in complex with CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient. CR3022 targets a highly conserved epitope that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding site can only be accessed when at least two RBDs on the trimeric S protein are in the "up" conformation. Overall, this study provides structural and molecular insight into the antigenicity of SARS-CoV-2. ONE SENTENCE SUMMARYStructural study of a cross-reactive SARS antibody reveals a conserved epitope on the SARS-CoV-2 receptor-binding domain. | |
| Science (New York, N.Y.) | |
| 2020 | |
| Artículo | |
| https://www.biorxiv.org/content/10.1101/2020.03.13.991570v1.full.pdf | |
| Inglés | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Artículos científicos |
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| 1107027.pdf | 2.88 MB | Adobe PDF | Visualizar/Abrir |