Structural basis for the evolution and antibody evasion of SARS-CoV-2 BA.2.86 and JN.1 subvariants
文献类型： 外文期刊
作者： Yang, Haonan 1 ; Guo, Huimin 2 ; Wang, Aojie 1 ; Cao, Liwei 1 ; Fan, Qing 2 ; Jiang, Jie 2 ; Wang, Miao 2 ; Lin, Lin 5 ; Ge, Xiangyang 2 ; Wang, Haiyan 2 ; Zhang, Runze 1 ; Liao, Ming 6 ; Yan, Renhong 1 ; Ju, Bin 2 ; Zhang, Zheng 2 ;
作者机构： 1.Southern Univ Sci & Technol, Key Univ Lab Metab & Hlth Guangdong, Inst Biol Electron Microscopy, Sch Med,Dept Biochem, Shenzhen, Guangdong, Peoples R China
2.Shenzhen Third Peoples Hosp, Inst Hepatol, Natl Clin Res Ctr Infect Dis, Shenzhen, Guangdong, Peoples R China
3.Southern Univ Sci & Technol, Affiliated Hosp 2, Sch Med, Shenzhen, Guangdong, Peoples R China
4.South China Agr Univ, Coll Vet Med, Guangdong Prov Key Lab Zoonosis Prevent & Control, Guangzhou, Guangdong, Peoples R China
5.Southern Univ Sci & Technol, Sustech Core Res Facil, Shenzhen, Guangdong, Peoples R China
6.Zhong Kai Univ Agr & Engn, Coll Anim Sci & Technol, Guangzhou, Guangdong, Peoples R China
7.Guangdong Acad Agr Sci, Inst Anim Hlth, Key Lab Livestock Dis Prevent Guangdong Prov, Guangzhou, Guangdong, Peoples R China
8.Guangdong Key Lab Antiinfect Drug Qual Evaluat, Shenzhen, Guangdong, Peoples R China
9.Chinese Acad Med Sci, Shenzhen Res Ctr Communicable Dis Diag & Treatment, Shenzhen, Guangdong, Peoples R China
期刊名称：NATURE COMMUNICATIONS （ 影响因子：15.7； 五年影响因子：17.2 ）
ISSN：
年卷期： 2024 年 15 卷 1 期
页码：
收录情况： SCI
摘要： The Omicron subvariants of SARS-CoV-2, especially for BA.2.86 and JN.1, have rapidly spread across multiple countries, posing a significant threat in the ongoing COVID-19 pandemic. Distinguished by 34 additional mutations on the Spike (S) protein compared to its BA.2 predecessor, the implications of BA.2.86 and its evolved descendant, JN.1 with additional L455S mutation in receptor-binding domains (RBDs), are of paramount concern. In this work, we systematically examine the neutralization susceptibilities of SARS-CoV-2 Omicron subvariants and reveal the enhanced antibody evasion of BA.2.86 and JN.1. We also determine the cryo-EM structures of the trimeric S proteins from BA.2.86 and JN.1 in complex with the host receptor ACE2, respectively. The mutations within the RBDs of BA.2.86 and JN.1 induce a remodeling of the interaction network between the RBD and ACE2. The L455S mutation of JN.1 further induces a notable shift of the RBD-ACE2 interface, suggesting the notably reduced binding affinity of JN.1 than BA.2.86. An analysis of the broadly neutralizing antibodies possessing core neutralizing epitopes reveals the antibody evasion mechanism underlying the evolution of Omicron BA.2.86 subvariant. In general, we construct a landscape of evolution in virus-receptor of the circulating Omicron subvariants. Here, the authors evaluate the neutralization susceptibilities of BA.2.86 and JN.1 and determine the structural basis for binding to the ACE2 receptor and monoclonal neutralizing antibodies, revealing their evolution and antibody evasion mechanism.
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