气候变化领域集成服务门户(CCPortal): Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

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DOI	10.1126/science.aax0902
	Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
	Wrapp D.; Wang N.; Corbett K.S.; Goldsmith J.A.; Hsieh C.-L.; Abiona O.; Graham B.S.; McLellan J.S.
发表日期	2020
ISSN	0036-8075
起始页码	1260
结束页码	1263
卷号	367 期号:6483
英文摘要	The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis. © 2020 American Association for the Advancement of Science. All rights reserved.
关键词	2019 nCoV S protein angiotensin converting enzyme 2 unclassified drug viral protein angiotensin converting enzyme 2 coronavirus spike glycoprotein dipeptidyl carboxypeptidase monoclonal antibody protein binding severe acute respiratory syndrome coronavirus 2 virus antibody virus receptor antibody detection method electron microscopy protein public health severe acute respiratory syndrome virus Article binding affinity biophysics corona virus disease 2019 coronavirus disease 2019 Coronavirus infection cross reaction cryoelectron microscopy molecular dynamics nonhuman priority journal protein binding protein structure SARS coronavirus Severe acute respiratory syndrome coronavirus 2 virus transmission virus virulence Betacoronavirus chemistry cryoelectron microscopy image processing immunology metabolism molecular model protein conformation protein domain protein multimerization ultrastructure Coronavirus SARS coronavirus Antibodies, Monoclonal Antibodies, Viral Betacoronavirus Cross Reactions Cryoelectron Microscopy Image Processing, Computer-Assisted Models, Molecular Peptidyl-Dipeptidase A Protein Binding Protein Conformation Protein Domains Protein Multimerization 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/133638
推荐引用方式 GB/T 7714	Wrapp D.,Wang N.,Corbett K.S.,et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation[J]. Science,2020,367(6483).
APA	Wrapp D..,Wang N..,Corbett K.S..,Goldsmith J.A..,Hsieh C.-L..,...&McLellan J.S..(2020).Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.,367(6483).
MLA	Wrapp D.,et al."Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation".367.6483(2020).