A human neutralizing antibody targets the receptor binding site of SARS-CoV-2.

Shi, Rui; Shan, Chao; Duan, Xiaomin; Chen, Zhihai; Liu, Peipei; Song, Jinwen; Song, Tao; Bi, Xiaoshan; Han, Chao; Wu, Lianao; Gao, Ge; Hu, Xue; Zhang, Yanan; Tong, Zhou; Huang, Weijin; Liu, William Jun; Wu, Guizhen; Zhang, Bo; Wang, Lan; Qi, Jianxun; Feng, Hui; Wang, Fu-Sheng; Wang, Qihui; Gao, George Fu; Yuan, Zhiming; Yan, Jinghua

An outbreak of the coronavirus disease 2019 (COVID-19)1-3, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)4 spread globally. Countermeasures are needed to treat and prevent further dissemination of the virus. In this study, we report the isolation of 2 specific human monoclonal antibodies (MAbs) from a convalescent COVID-19 patient. CA1 and CB6 demonstrated potent SARS-CoV-2-specific neutralization activity in vitro against SARS-CoV-2. In addition, CB6 inhibited SARS-CoV-2 infection in rhesus monkeys at both prophylactic and treatment settings. Further structural studies revealed that CB6 recognizes an epitope that overlaps with angiotensin converting enzyme 2 (ACE2)-binding sites in SARS-CoV-2 receptor binding domain (RBD), thereby interfering with the virus/receptor interactions by both steric hindrance and direct interface-residue competition. Our results suggest CB6 deserves further clinical translation.