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A non-competing pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2

By Yan Wu, Feiran Wang, Chenguang Shen, Weiyu Peng, Delin Li, Cheng Zhao, Zhaohui Li, Shihua Li, Yuhai Bi, Yang Yang, Yuhuan Gong, Haixia Xiao, Zheng Fan, Shuguang Tan, Guizhen Wu, Wenjie Tan, Xuancheng Lu, Changfa Fan, Qihui Wang, Yingxia Liu, Jianxun Qi, George Fu Gao, Feng Gao, Lei Liu

Posted 07 May 2020
medRxiv DOI: 10.1101/2020.05.01.20077743

Neutralizing antibodies could be antivirals against COVID-19 pandemics. Here, we report the isolation of four human-origin monoclonal antibodies from a convalescent patient in China. All of these isolated antibodies display neutralization abilities in vitro. Two of them (B38 and H4) block the binding between RBD and vial cellular receptor ACE2. Further competition assay indicates that B38 and H4 recognize different epitopes on the RBD, which is ideal for a virus-targeting mAb-pair to avoid immune escape in the future clinical applications. Moreover, therapeutic study on the mouse model validated that these two antibodies can reduce virus titers in the infected mouse lungs. Structure of RBD-B38 complex revealed that most residues on the epitope are overlapped with the RBD-ACE2 binding interface, which explained the blocking efficacy and neutralizing capacity. Our results highlight the promise of antibody-based therapeutics and provide the structural basis of rational vaccine design.

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