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A potent human monoclonal antibody with pan-neutralizing activities directly dislocates S trimer of SARS-CoV-2 through binding both up and down forms of RBD

By Xiaofei Wang, Ao Hu, Xiangyu Chen, Yixin Zhang, Fei Yu, Shuai Yue, Arong Li, Junsong Zhang, Zhiwei Pan, Yang Yang, Yao Lin, Leiqiong Gao, Jing Zhou, Jing Zhao, Fang Li, Yaling Shi, Feng Huang, Xiaofan Yang, Yi Peng, Luoyang Tu, Huan Zhang, Huanying Zheng, Jun He, Hui Zhang, Lifan Xu, Qizhao Huang, Yongqun Zhu, Kai Deng, Lilin Ye

Posted 30 Nov 2021
bioRxiv DOI: 10.1101/2021.11.29.470356

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused a global pandemic of novel corona virus disease (COVID-19). The neutralizing monoclonal antibodies (mAbs) targeting the receptor binding domain (RBD) of SARS-CoV-2 are among the most promising strategies to prevent and treat COVID-19. However, SARS-CoV-2 variants of concern (VOCs) profoundly reduced the efficacies of most of mAbs and vaccines approved for clinical use. Herein, we demonstrated mAb 35B5 efficiently neutralizes both wild-type (WT) SARS-CoV-2 and VOCs, including B.1.617.2 (delta) variant, in vitro and in vivo. Cryo-electron microscopy (cryo-EM) revealed that 35B5 neutralizes SARS-CoV-2 by targeting a unique epitope that avoids the prevailing mutation sites on RBD identified in circulating VOCs, providing the molecular basis for its pan-neutralizing efficacy. The 35B5-binding epitope could also be exploited for the rational design of a universal SARS-CoV-2 vaccine.

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