气候变化领域集成服务门户(CCPortal): A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV

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DOI	10.1126/science.abb7269
	A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
	Yuan M.; Wu N.C.; Zhu X.; Lee C.-C.D.; So R.T.Y.; Lv H.; Mok C.K.P.; Wilson I.A.
发表日期	2020
ISSN	0036-8075
起始页码	630
结束页码	633
卷号	368 期号:6491
英文摘要	The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the “up” conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2. Copyright © 2020 The Authors,
关键词	angiotensin converting enzyme 2 epitope neutralizing antibody virus hemagglutinin virus spike protein angiotensin converting enzyme 2 coronavirus receptors coronavirus spike glycoprotein dipeptidyl carboxypeptidase epitope neutralizing antibody spike glycoprotein, SARS-CoV spike protein, SARS-CoV-2 virus antibody virus antigen virus receptor antibody antigen chemical binding crystal structure protein respiratory disease viral disease virus amino terminal sequence antibody isolation antigen binding antigenicity Article binding affinity binding site conservation biology controlled study coronavirus disease 2019 cross reaction cryoelectron microscopy crystal structure enzyme linked immunosorbent assay epidemic glycosylation human hydrophobicity immune response in vitro study in vivo study light chain nonhuman priority journal protein conformation protein domain protein interaction protein localization protein structure protein targeting receptor binding SARS coronavirus Severe acute respiratory syndrome coronavirus 2 amino acid sequence antibody affinity Betacoronavirus binding site chemistry immunology metabolism molecular model SARS coronavirus X ray crystallography Coronavirus SARS coronavirus Amino Acid Sequence Antibodies, Neutralizing Antibodies, Viral Antibody Affinity Antigens, Viral Betacoronavirus Binding Sites Cross Reactions Crystallography, X-Ray Epitopes Models, Molecular Peptidyl-Dipeptidase A Protein Conformation Protein Domains Protein Interaction Domains and Motifs Receptors, Virus SARS Virus Spike Glycoprotein, Coronavirus
语种	英语
来源机构	Science
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/133519
推荐引用方式 GB/T 7714	Yuan M.,Wu N.C.,Zhu X.,et al. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV[J]. Science,2020,368(6491).
APA	Yuan M..,Wu N.C..,Zhu X..,Lee C.-C.D..,So R.T.Y..,...&Wilson I.A..(2020).A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV.,368(6491).
MLA	Yuan M.,et al."A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV".368.6491(2020).