An ultrapotent pan-β-coronavirus lineage B (β-CoV-B) neutralizing antibody locks the receptor-binding domain in closed conformation by targeting its conserved epitope

doi:10.1007/s13238-021-00871-6

Protein Cell

2022, Vol. 13

Issue (9) : 655-675 https://doi.org/10.1007/s13238-021-00871-6

RESEARCH ARTICLE

An ultrapotent pan-β-coronavirus lineage B (β-CoV-B) neutralizing antibody locks the receptor-binding domain in closed conformation by targeting its conserved epitope

Zezhong Liu¹, Wei Xu¹, Zhenguo Chen¹, Wangjun Fu², Wuqiang Zhan¹, Yidan Gao¹, Jie Zhou¹, Yunjiao Zhou¹, Jianbo Wu¹, Qian Wang¹, Xiang Zhang¹, Aihua Hao¹, Wei Wu¹, Qianqian Zhang¹, Yaming Li¹, Kaiyue Fan², Ruihong Chen², Qiaochu Jiang¹, Christian T. Mayer³, Till Schoofs⁴, Youhua Xie¹, Shibo Jiang¹, Yumei Wen¹, Zhenghong Yuan¹(

), Kang Wang²(

), Lu Lu¹(

), Lei Sun¹(

), Qiao Wang¹(

)

¹. Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences; Shanghai Institute of Infectious Disease and Biosecurity; the Fifth People’s Hospital of Shanghai; Shanghai Key Laboratory of Medical Epigenetics, International Co-laboratory of Medical Epigenetics and Metabolism (Ministry of Science and Technology); Institutes of Biomedical Sciences; Biosafety Level 3 Laboratory, Shanghai Medical College, Fudan University, Shanghai 200032, China
². CAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
³. Experimental Immunology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
⁴. GSK Vaccines, 1300 Wavre, Belgium

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Abstract

New threats posed by the emerging circulating variants of SARS-CoV-2 highlight the need to find conserved neutralizing epitopes for therapeutic antibodies and efficient vaccine design. Here, we identified a receptor-binding domain (RBD)-binding antibody, XG014, which potently neutralizes β-coronavirus lineage B (β-CoV-B), including SARS-CoV-2, its circulating variants, SARS-CoV and bat SARSr-CoV WIV1. Interestingly, antibody family members competing with XG014 binding show reduced levels of cross-reactivity and induce antibody-dependent SARS-CoV-2 spike (S) protein-mediated cell-cell fusion, suggesting a unique mode of recognition by XG014. Structural analyses reveal that XG014 recog-nizes a conserved epitope outside the ACE2 binding site and completely locks RBD in the non-functional “down” conformation, while its family member XG005 directly competes with ACE2 binding and position the RBD “up”. Single administration of XG014 is effective in protection against and therapy of SARS-CoV-2 infection in vivo. Our findings suggest the potential to develop XG014 as pan-β-CoV-B therapeutics and the importance of the XG014 conserved antigenic epitope for designing broadly protective vaccines against β-CoV-B and newly emerging SARS-CoV-2 variants of concern.

Keywords SARS-CoV-2 neutralizing antibody receptor-binding domain XG014 antibody-dependent cell-cell fusion

Corresponding Author(s): Zhenghong Yuan,Kang Wang,Lu Lu,Lei Sun,Qiao Wang

About author:

Tongcan Cui and Yizhe Hou contributed equally to this work.

Online First Date: 23 November 2021 Issue Date: 09 August 2022

Cite this article:

Zezhong Liu,Wei Xu,Zhenguo Chen, et al. An ultrapotent pan-β-coronavirus lineage B (β-CoV-B) neutralizing antibody locks the receptor-binding domain in closed conformation by targeting its conserved epitope[J]. Protein Cell, 2022, 13(9): 655-675.

URL:

https://academic.hep.com.cn/pac/EN/10.1007/s13238-021-00871-6
https://academic.hep.com.cn/pac/EN/Y2022/V13/I9/655

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