典型文献
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
文献摘要：
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 neutralizesβ-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.
文献关键词：
中图分类号：
作者姓名：
Zezhong Liu;Wei Xu;Zhenguo Chen;Wangjun Fu;Wuqiang Zhan;Yidan Gao;Jie Zhou;Yunjiao Zhou;Jianbo Wu;Qian Wang;Xiang Zhang;Aihua Hao;Wei Wu;Qianqian Zhang;Yarning Li;Kaiyue Fan;Ruihong Chen;Qiaochu Jiang;Christian T.Mayer;Till Schoofs;Youhua Xie;Shibo Jiang;Yumei Wen;Zhenghong Yuan;Kang Wang;Lu Lu;Lei Sun;Qiao Wang
作者机构：
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;CAS Key Laboratory of Infection and Immunity,National Laboratory of Macromolecules,Institute of Biophysics,Chinese Academy of Sciences,Beijing 100101,China;Experimental Immunology Branch,Center for Cancer Research,National Cancer Institute,National Institutes of Health,Bethesda,MD 20892,USA;GSK Vaccines,1300 Wavre,Belgium
文献出处：
引用格式：
[1]Zezhong Liu;Wei Xu;Zhenguo Chen;Wangjun Fu;Wuqiang Zhan;Yidan Gao;Jie Zhou;Yunjiao Zhou;Jianbo Wu;Qian Wang;Xiang Zhang;Aihua Hao;Wei Wu;Qianqian Zhang;Yarning Li;Kaiyue Fan;Ruihong Chen;Qiaochu Jiang;Christian T.Mayer;Till Schoofs;Youhua Xie;Shibo Jiang;Yumei Wen;Zhenghong Yuan;Kang Wang;Lu Lu;Lei Sun;Qiao Wang-.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].蛋白质与细胞,2022(09):655-675
A类：
ultrapotent,XG014,neutralizes,SARSr,WIV1,nizes,XG005
B类：
An,pan,coronavirus,lineage,CoV,neutralizing,antibody,locks,receptor,binding,domain,closed,conformation,by,targeting,its,conserved,New,threats,posed,emerging,circulating,variants,highlight,need,epitopes,antibodies,efficient,Here,we,identified,RBD,which,potently,including,bat,Interestingly,family,members,competing,show,reduced,levels,cross,reactivity,induce,dependent,spike,protein,mediated,cell,fusion,suggesting,unique,mode,recognition,Structural,analyses,reveal,that,outside,ACE2,site,completely,functional,down,while,directly,competes,position,up,Single,administration,effective,protection,against,therapy,infection,vivo,Our,findings,potential,develop,as,therapeutics,importance,antigenic,designing,broadly,protective,vaccines,newly,concern
AB值：
0.481145
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