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Lv, Zhe; Deng, Yong-Qiang; Ye, Qing; Cao, Lei; Sun, Chun-Yun; Fan, Changfa; Huang, Weijin; Sun, Shihui; Sun, Yao; Zhu, Ling; Chen, Qi; Wang, Nan; Nie, Jianhui; Cui, Zhen; Zhu, Dandan; Shaw, Neil; Li, Xiao-Feng; Li, Qianqian; Xie, Liangzhi; Wang, Youchun; Rao, Zihe; Qin, Cheng-Feng; Wang, Xiangxi
Science, 09/2020, Volume: 369, Issue: 6510Journal Article
The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in an unprecedented public health crisis. There are no approved vaccines or therapeutics for treating COVID-19. Here we report a humanized monoclonal antibody, H014, that efficiently neutralizes SARS-CoV-2 and SARS-CoV pseudoviruses as well as authentic SARS-CoV-2 at nanomolar concentrations by engaging the spike (S) receptor binding domain (RBD). H014 administration reduced SARS-CoV-2 titers in infected lungs and prevented pulmonary pathology in a human angiotensin-converting enzyme 2 mouse model. Cryo-electron microscopy characterization of the SARS-CoV-2 S trimer in complex with the H014 Fab fragment unveiled a previously uncharacterized conformational epitope, which was only accessible when the RBD was in an open conformation. Biochemical, cellular, virological, and structural studies demonstrated that H014 prevents attachment of SARS-CoV-2 to its host cell receptors. Epitope analysis of available neutralizing antibodies against SARS-CoV and SARS-CoV-2 uncovered broad cross-protective epitopes. Our results highlight a key role for antibody-based therapeutic interventions in the treatment of COVID-19.
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