Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants

Tingting Li, Wenhui Xue, Qingbing Zheng, Shuo Song, Chuanlai Yang, Hualong Xiong, Sibo Zhang, Minqing Hong, Yali Zhang, Hai Yu, Yuyun Zhang, Hui Sun, Yang Huang, Tingting Deng, Xin Chi, Jinjin Li, Shaojuan Wang, Lizhi Zhou, Tingting Chen, Yingbin Wang, Tong Cheng, Tianying Zhang, Quan Yuan, Qinjian Zhao, Jun Zhang, Jason S. McLellan, Z. Hong Zhou (), Zheng Zhang (), Shaowei Li (), Ying Gu () and Ningshao Xia ()
Additional contact information
Tingting Li: Xiamen University
Wenhui Xue: Xiamen University
Qingbing Zheng: Xiamen University
Shuo Song: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital
Chuanlai Yang: Xiamen University
Hualong Xiong: Xiamen University
Sibo Zhang: Xiamen University
Minqing Hong: Xiamen University
Yali Zhang: Xiamen University
Hai Yu: Xiamen University
Yuyun Zhang: Xiamen University
Hui Sun: Xiamen University
Yang Huang: Xiamen University
Tingting Deng: Xiamen University
Xin Chi: Xiamen University
Jinjin Li: Xiamen University
Shaojuan Wang: Xiamen University
Lizhi Zhou: Xiamen University
Tingting Chen: Xiamen University
Yingbin Wang: Xiamen University
Tong Cheng: Xiamen University
Tianying Zhang: Xiamen University
Quan Yuan: Xiamen University
Qinjian Zhao: Xiamen University
Jun Zhang: Xiamen University
Jason S. McLellan: The University of Texas at Austin
Z. Hong Zhou: California NanoSystems Institute (CNSI), UCLA
Zheng Zhang: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital
Shaowei Li: Xiamen University
Ying Gu: Xiamen University
Ningshao Xia: Xiamen University

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract The emergence of numerous variants of SARS-CoV-2, the causative agent of COVID-19, has presented new challenges to the global efforts to control the COVID-19 pandemic. Here, we obtain two cross-neutralizing antibodies (7D6 and 6D6) that target Sarbecoviruses’ receptor-binding domain (RBD) with sub-picomolar affinities and potently neutralize authentic SARS-CoV-2. Crystal structures show that both antibodies bind a cryptic site different from that recognized by existing antibodies and highly conserved across Sarbecovirus isolates. Binding of these two antibodies to the RBD clashes with the adjacent N-terminal domain and disrupts the viral spike. Both antibodies confer good resistance to mutations in the currently circulating SARS-CoV-2 variants. Thus, our results have direct relevance to public health as options for passive antibody therapeutics and even active prophylactics. They can also inform the design of pan-sarbecovirus vaccines.

Date: 2021
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DOI: 10.1038/s41467-021-25997-3

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