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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.
Cell; 181(4): 894-904.e9, 2020 05 14.
Artículo en Inglés | MEDLINE | ID: mdl-32275855
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.