Humanized single domain antibodies neutralize SARS-CoV-2 by targeting the spike receptor binding domain

Xiaojing Chi, Xiuying Liu, Conghui Wang, Xinhui Zhang, Xiang Li, Jianhua Hou, Lili Ren, Qi Jin (), Jianwei Wang () and Wei Yang ()
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Xiaojing Chi: Chinese Academy of Medical Sciences and Peking Union Medical College
Xiuying Liu: Chinese Academy of Medical Sciences and Peking Union Medical College
Conghui Wang: Chinese Academy of Medical Sciences and Peking Union Medical College
Xinhui Zhang: Chinese Academy of Medical Sciences and Peking Union Medical College
Xiang Li: Beijing Kawin Technology Co., Ltd.
Jianhua Hou: Beijing Kawin Technology Co., Ltd.
Lili Ren: Chinese Academy of Medical Sciences and Peking Union Medical College
Qi Jin: Chinese Academy of Medical Sciences and Peking Union Medical College
Jianwei Wang: Chinese Academy of Medical Sciences and Peking Union Medical College
Wei Yang: Chinese Academy of Medical Sciences and Peking Union Medical College

Nature Communications, 2020, vol. 11, issue 1, 1-7

Abstract: Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spreads worldwide and leads to an unprecedented medical burden and lives lost. Neutralizing antibodies provide efficient blockade for viral infection and are a promising category of biological therapies. Here, using SARS-CoV-2 spike receptor-binding domain (RBD) as a bait, we generate a panel of humanized single domain antibodies (sdAbs) from a synthetic library. These sdAbs reveal binding kinetics with the equilibrium dissociation constant (KD) of 0.99–35.5 nM. The monomeric sdAbs show half maximal neutralization concentration (EC50) of 0.0009–0.07 µg/mL and 0.13–0.51 µg/mL against SARS-CoV-2 pseudotypes, and authentic SARS-CoV-2, respectively. Competitive ligand-binding experiments suggest that the sdAbs either completely block or significantly inhibit the association between SARS-CoV-2 RBD and viral entry receptor ACE2. Fusion of the human IgG1 Fc to sdAbs improve their neutralization activity by up to ten times. These results support neutralizing sdAbs as a potential alternative for antiviral therapies.

Date: 2020
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DOI: 10.1038/s41467-020-18387-8

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