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

Li, Tingting1,2; Xue, Wenhui1,2; Zheng, Qingbing1,2; Song, Shuo3,4; Yang, Chuanlai1,2; Xiong, Hualong1,2; Zhang, Sibo1,2; Hong, Minqing1,2; Zhang, Yali1,2; Yu, Hai1,2; Zhang, Yuyun1,2; Sun, Hui1,2; Huang, Yang1,2; Deng, Tingting1,2; Chi, Xin1,2; Li, Jinjin1,2; Wang, Shaojuan1,2; Zhou, Lizhi1,2; Chen, Tingting1,2; Wang, Yingbin1,2; Cheng, Tong1,2; Zhang, Tianying1,2; Yuan, Quan1,2; Zhao, Qinjian1,2; Zhang, Jun1,2; McLellan, Jason S.5; Zhou, Z. Hong6,7; Zhang, Zheng3,4; Li, Shaowei1,2; Gu, Ying1,2; Xia, Ningshao1,2,8

2021-09-27

10.1038/s41467-021-25997-3

NATURE COMMUNICATIONS   影响因子和分区

2041-1723

["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.","Antibodies (Abs) targeting highly conserved epitopes are important tools against emerging virus variants. Here, the authors characterize Abs that recognize a cryptic epitope in the receptor-binding domain of SARS-CoV-2 spike that is well conserved and show that these Abs can neutralize several variants of concerns."]

SCI

英语

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通讯

National Natural Science Foundation of China[82001756,81991491,"U1705283"]

Science & Technology - Other Topics

Multidisciplinary Sciences

WOS:000700605800015

NATURE PORTFOLIO

Web of Science

1.Xiamen Univ, Sch Life Sci, Sch Publ Hlth, State Key Lab Mol Vaccinol & Mol Diagnost, Xiamen 361102, Fujian, Peoples R China
2.Xiamen Univ, Natl Inst Diagnost & Vaccine Dev Infect Dis, Xiamen 361102, Fujian, Peoples R China
3.Shenzhen Third Peoples Hosp, Natl Clin Res Ctr Infect Dis, Inst Hepatol, Shenzhen 518112, Guangdong, Peoples R China
4.Southern Univ Sci & Technol, Sch Med, Affiliated Hosp 2, Shenzhen 518112, Guangdong, Peoples R China
5.Univ Texas Austin, Dept Mol Biosci, Austin, TX 78712 USA
6.Univ Calif Los Angeles, Calif NanoSyst Inst CNSI, Los Angeles, CA 90095 USA
7.Univ Calif Los Angeles, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90095 USA
8.Chinese Acad Med Sci, Res Unit Frontier Technol Struct Vaccinol, Xiamen 518112, Fujian, Peoples R China

Li, Tingting,Xue, Wenhui,Zheng, Qingbing,et al. Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants[J]. NATURE COMMUNICATIONS,2021,12(1).

Li, Tingting.,Xue, Wenhui.,Zheng, Qingbing.,Song, Shuo.,Yang, Chuanlai.,...&Xia, Ningshao.(2021).Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants.NATURE COMMUNICATIONS,12(1).

Li, Tingting,et al."Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants".NATURE COMMUNICATIONS 12.1(2021).