The neutralizing breadth of antibodies targeting diverse conserved epitopes between SARS-CoV and SARS-CoV-2

Author:

Xiong Hualong1,Sun Hui1,Wang Siling1,Yuan Lunzhi1,Liu Liqin1,Zhu Yuhe1,Zhang Jinlei1,Huang Yang1,Qi Ruoyao1,Jiang Yao1,Ma Jian1,Zhou Ming1,Ma Yue1,Fu Rao1,Yan Siping1,Yue Mingxi1,Wu Yangtao1,Wei Min1,Wang Yizhen1,Li Tingting1,Wang Yingbin1,Zheng Zizheng1,Yu Hai1,Cheng Tong1ORCID,Li Shaowei1,Yuan Quan12,Zhang Jun1,Guan Yi23,Zheng Qingbing1ORCID,Zhang Tianying1,Xia Ningshao14ORCID

Affiliation:

1. State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Public Health, School of Life Sciences, Xiamen University, Xiamen 361102, China

2. Guangdong-Hongkong Joint Laboratory of Emerging Infectious Diseases/Joint Laboratory for International Collaboration in Virology and Emerging Infectious Diseases, Joint Institute of Virology (Shantou University and University of Hong Kong), Shantou University, Shantou 515063, China

3. State Key Laboratory of Emerging Infectious Diseases, University of Hong Kong, Hong Kong 999077, China

4. Research Unit of Frontier Technology of Structural Vaccinology, Chinese Academy of Medical Sciences, Xiamen 361102, China

Abstract

Antibody therapeutics for the treatment of COVID-19 have been highly successful. However, the recent emergence of the Omicron variant has posed a challenge, as it evades detection by most existing SARS-CoV-2 neutralizing antibodies (nAbs). Here, we successfully generated a panel of SARS-CoV-2/SARS-CoV cross-neutralizing antibodies by sequential immunization of the two pseudoviruses. Of the potential candidates, we found that nAbs X01, X10, and X17 offer broad neutralizing potential against most variants of concern, with X17 further identified as a Class 5 nAb with undiminished neutralization against the Omicron variant. Cryo-electron microscopy structures of the three antibodies together in complex with each of the spike proteins of the prototypical SARS-CoV, SARS-CoV-2, and Delta and Omicron variants of SARS-CoV-2 defined three nonoverlapping conserved epitopes on the receptor-binding domain. The triple-antibody mixture exhibited enhanced resistance to viral evasion and effective protection against infection of the Beta variant in hamsters. Our findings will aid the development of antibody therapeutics and broad vaccines against SARS-CoV-2 and its emerging variants.

Funder

National Natural Science Foundation of China

Fujian Natural Science Foundation for Distinguished Yong Scholars

Xiamen Youth Innovation Fund Project

Bill & Melinda Gates Foundation

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

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