Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody

• DOI: 10.1126/science.abc5881
• Publication Date: 2020-07-23T23:09:44Z
• Authors: Zhe Lv; Yong-Qiang Deng; Qing Ye; Lei Cao; Chun-Yun Sun; Changfa Fan; Weijin Huang; Shihui Sun; Yao Sun; Ling Zhu; Qi Chen; Nan Wang; Jianhui Nie; Zhen Cui; Dandan Zhu; Neil Shaw; Xiao-Feng Li; Qianqian Li; Liangzhi Xie; Youchun Wang; Zihe Rao; Cheng-Feng Qin; Xiangxi Wang
• Keywords: 0301 basic medicine; Pneumonia, Viral; Peptidyl-Dipeptidase A; Antibodies, Monoclonal, Humanized; Betacoronavirus; Immunoglobulin Fab Fragments; Mice; 03 medical and health sciences; Protein Domains; Chlorocebus aethiops; Animals; Humans; Lung; Pandemics; Multidisciplinary; COVID-19; Antibodies, Neutralizing; 3. Good health; Severe acute respiratory syndrome-related coronavirus; Receptors, Virus; Angiotensin-Converting Enzyme 2; Protein Multimerization; Coronavirus Infections; Epitope Mapping; Reports

A steric block to SARS-CoV-2

In response to infection by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the immune system makes antibodies, many of which target the spike protein, a key player in host cell entry. Antibodies that potently neutralize the virus hold promise as therapeutics and could inform vaccine design. Lv et al. report a humanized monoclonal antibody that protected against SARS-CoV-2 in a mouse model. The cryo–electron microscopy structure, together with biochemical, cellular, and virological studies, showed that the antibody acts by binding to the receptor-binding domain of the spike and blocking its attachment to the host receptor.

Science , this issue p. 1505