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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/3671| Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2 | |
| Wang Qihui. Zhang Yanfang. Wu Lili. Niu Sheng. Song Chunli. Zhang Zengyuan. Lu Guangwen. Qiao Chengpeng. Hu Yu. Yuen Kwok-Yung. Wang Qisheng. Zhou Huan. Yan Jinghua. Qi Jianxun. | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| 10.1016/j.cell.2020.03.045 | |
| The recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus. | |
| Cell | |
| 2020 | |
| Artículo | |
| https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7144619/pdf/main.pdf | |
| Inglés | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Artículos científicos |
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