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. 2020 Aug;584(7819):115-119.
doi: 10.1038/s41586-020-2380-z. Epub 2020 May 26.

Human neutralizing antibodies elicited by SARS-CoV-2 infection

Bin Ju #  1   2 , Qi Zhang #  3 , Jiwan Ge #  4 , Ruoke Wang  3 , Jing Sun  5 , Xiangyang Ge  1 , Jiazhen Yu  1 , Sisi Shan  3 , Bing Zhou  1 , Shuo Song  1 , Xian Tang  1 , Jinfang Yu  4 , Jun Lan  4 , Jing Yuan  6 , Haiyan Wang  1 , Juanjuan Zhao  1   2 , Shuye Zhang  7 , Youchun Wang  8 , Xuanling Shi  3 , Lei Liu  1   2 , Jincun Zhao  5 , Xinquan Wang  9 , Zheng Zhang  10   11 , Linqi Zhang  12
Affiliations

Human neutralizing antibodies elicited by SARS-CoV-2 infection

Bin Ju et al. Nature. 2020 Aug.

Abstract

The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) presents a global health emergency that is in urgent need of intervention1-3. The entry of SARS-CoV-2 into its target cells depends on binding between the receptor-binding domain (RBD) of the viral spike protein and its cellular receptor, angiotensin-converting enzyme 2 (ACE2)2,4-6. Here we report the isolation and characterization of 206 RBD-specific monoclonal antibodies derived from single B cells from 8 individuals infected with SARS-CoV-2. We identified antibodies that potently neutralize SARS-CoV-2; this activity correlates with competition with ACE2 for binding to RBD. Unexpectedly, the anti-SARS-CoV-2 antibodies and the infected plasma did not cross-react with the RBDs of SARS-CoV or Middle East respiratory syndrome-related coronavirus (MERS-CoV), although there was substantial plasma cross-reactivity to their trimeric spike proteins. Analysis of the crystal structure of RBD-bound antibody revealed that steric hindrance inhibits viral engagement with ACE2, thereby blocking viral entry. These findings suggest that anti-RBD antibodies are largely viral-species-specific inhibitors. The antibodies identified here may be candidates for development of clinical interventions against SARS-CoV-2.

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