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题名

Identification of a highly conserved neutralizing epitope within the RBD region of diverse SARS-CoV-2 variants

作者
通讯作者Lan,Wang; Changlin,Dou; Zheng,Liu; Jincun,Zhao
共同第一作者An,Yan; Deyong,Song; Maoqin,Duan; Chuangchuang,Dong
发表日期
2024-01-29
DOIhttps://doi.org/10.1038/s41467-024-45050-3
发表期刊
ISSN
2041-1723
EISSN
2041-1723
卷号15期号:1页码:842
摘要

The constant emergence of SARS-CoV-2 variants continues to impair the efficacy of existing neutralizing antibodies, especially XBB.1.5 and EG.5, which showed exceptional immune evasion properties. Here, we identify a highly conserved neutralizing epitope targeted by a broad-spectrum neutralizing antibody BA7535, which demonstrates high neutralization potency against not only previous variants, such as Alpha, Beta, Gamma, Delta and Omicron BA.1-BA.5, but also more recently emerged Omicron subvariants, including BF.7, CH.1.1, XBB.1, XBB.1.5, XBB.1.9.1, EG.5. Structural analysis of the Omicron Spike trimer with BA7535-Fab using cryo-EM indicates that BA7535 recognizes a highly conserved cryptic receptor-binding domain (RBD) epitope, avoiding most of the mutational hot spots in RBD. Furthermore, structural simulation based on the interaction of BA7535-Fab/RBD complexes dissects the broadly neutralizing effect of BA7535 against latest variants. Therapeutic and prophylactic treatment with BA7535 alone or in combination with BA7208 protected female mice from the circulating Omicron BA.5 and XBB.1 variant infection, suggesting the highly conserved neutralizing epitope serves as a potential target for developing highly potent therapeutic antibodies and vaccines.

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英语
学校署名
共同第一 ; 通讯
出版者
Scopus记录号
2-s2.0-85183399803
来源库
人工提交
全文链接https://www.nature.com/articles/s41467-024-45050-3
出版状态
正式出版
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成果类型期刊论文
条目标识符http://sustech.caswiz.com/handle/2SGJ60CL/677962
专题冷冻电镜中心
南方科技大学医学院
南方科技大学第二附属医院
作者单位
1.State Key Laboratory of Respiratory Disease, National Clinical Research Center for Respiratory Disease, Guangzhou Institute of Respiratory Health, the First Affiliated Hospital of Guangzhou Medical University, Guangzhou, China
2.Clinical Laboratory Medicine Department, The Second Affiliated Hospital of Guangzhou Medical University, Guangzhou, China
3.GMU-GIBH Joint School of Life Sciences, Guangzhou Medical University, Guangzhou, China
4.Cryo-electron Microscopy Center, Southern University of Science and Technology, Shenzhen, China
5.Antibody Research and Development Center, Shandong Boan Biotechnology Co., Ltd., Yantai, China
6.Division of Monoclonal Antibodies, Institute for Biological Product Control, National Institutes for Food and Drug Control (NIFDC), Beijing, China
7.Health and Quarantine Laboratory, Guangzhou Customs District Technology Centre, Guangzhou, China
8.Guangzhou National Laboratory, Bio-Island, Guangzhou, China
9.Shanghai Institute for Advanced Immunochemical Studies, School of Life Science and Technology, ShanghaiTech University, Shanghai, China
10.Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital; The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Shenzhen, China
通讯作者单位冷冻电镜中心;  南方科技大学医学院;  南方科技大学第二附属医院
推荐引用方式
GB/T 7714
Yanqun,Wang,An,Yan,Deyong,Song,et al. Identification of a highly conserved neutralizing epitope within the RBD region of diverse SARS-CoV-2 variants[J]. Nature Communications,2024,15(1):842.
APA
Yanqun,Wang.,An,Yan.,Deyong,Song.,Maoqin,Duan.,Chuangchuang,Dong.,...&Jincun,Zhao.(2024).Identification of a highly conserved neutralizing epitope within the RBD region of diverse SARS-CoV-2 variants.Nature Communications,15(1),842.
MLA
Yanqun,Wang,et al."Identification of a highly conserved neutralizing epitope within the RBD region of diverse SARS-CoV-2 variants".Nature Communications 15.1(2024):842.
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