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

2020; American Association for the Advancement of Science; Volume: 368; Issue: 6496 Linguagem: Inglês

10.1126/science.abc2241

1095-9203

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, Chen Zhang, Jianxun Qi, George F. Gao, Feng Gao, Lei Liu,

COVID-19 Impact on Reproduction

Neutralizing antibodies could potentially be used as antivirals against the coronavirus disease 2019 (COVID-19) pandemic. Here, we report isolation of four human-origin monoclonal antibodies from a convalescent patient, all of which display neutralization abilities. The antibodies B38 and H4 block binding between the spike glycoprotein receptor binding domain (RBD) of the virus and the cellular receptor angiotensin-converting enzyme 2 (ACE2). A competition assay indicated different epitopes on the RBD for these two antibodies, making them a potentially promising virus-targeting monoclonal antibody pair for avoiding 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.