REPORT
A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2
Yan Wu1,2,*,†, Feiran Wang3,4,*, Chenguang Shen3,5,*, Weiyu Peng3,6,*, Delin Li3,5,7,*, Cheng Zhao3,8, Zhaohui Li3,9, Shihua Li3, Yuhai Bi3,10, Yang Yang5, Yuhuan Gong3,10, Haixia Xiao7, Zheng Fan3, Shuguang Tan3, Guizhen Wu11, Wenjie Tan11, Xuancheng Lu12, Changfa Fan13, Qihui Wang3, Yingxia Liu5, Chen Zhang1, Jianxun Qi3, George Fu Gao3,†, Feng Gao7,†, Lei Liu5,†
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Science 13 May 2020:
eabc2241
DOI: 10.1126/science.abc2241
Abstract
Neutralizing antibodies could be antivirals against COVID-19 pandemics. Here, we report isolation of four human-origin monoclonal antibodies from a convalescent patient, all of which display neutralization abilities. B38 and H4 block the binding between virus S-protein RBD and cellular receptor ACE2. A competition assay indicates their different epitopes on the RBD, making them a potential virus-targeting MAb-pair to avoid immune escape in future clinical applications. Moreover, a therapeutic study in a mouse model validated that these antibodies can reduce virus titers in infected lungs. The RBD-B38 complex structure revealed that most residues on the epitope overlap with the RBD-ACE2 binding interface, explaining the blocking effect and neutralizing capacity. Our results highlight the promise of antibody-based therapeutics and provide a structural basis for rational vaccine design.