Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.
Identifieur interne : 000774 ( PubMed/Corpus ); précédent : 000773; suivant : 000775Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.
Auteurs : Daniel Wrapp ; Nianshuang Wang ; Kizzmekia S. Corbett ; Jory A. Goldsmith ; Ching-Lin Hsieh ; Olubukola Abiona ; Barney S. Graham ; Jason S. MclellanSource :
- Science (New York, N.Y.) [ 1095-9203 ] ; 2020.
English descriptors
- KwdEn :
- Antibodies, Monoclonal (immunology), Antibodies, Viral (immunology), Betacoronavirus (chemistry), Betacoronavirus (immunology), Betacoronavirus (metabolism), Betacoronavirus (ultrastructure), Cross Reactions, Cryoelectron Microscopy, Image Processing, Computer-Assisted, Models, Molecular, Peptidyl-Dipeptidase A (metabolism), Protein Binding, Protein Conformation, Protein Domains, Protein Multimerization, Receptors, Virus (metabolism), SARS Virus (chemistry), SARS Virus (immunology), SARS Virus (ultrastructure), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (immunology), Spike Glycoprotein, Coronavirus (metabolism), Spike Glycoprotein, Coronavirus (ultrastructure).
- MESH :
- chemical , chemistry : Spike Glycoprotein, Coronavirus.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Spike Glycoprotein, Coronavirus.
- chemistry : Betacoronavirus, SARS Virus.
- immunology : Betacoronavirus, SARS Virus.
- metabolism : Betacoronavirus, Peptidyl-Dipeptidase A, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- ultrastructure : Betacoronavirus, SARS Virus, Spike Glycoprotein, Coronavirus.
- Cross Reactions, Cryoelectron Microscopy, Image Processing, Computer-Assisted, Models, Molecular, Protein Binding, Protein Conformation, Protein Domains, Protein Multimerization.
Abstract
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.
DOI: 10.1126/science.abb2507
PubMed: 32075877
Links to Exploration step
pubmed:32075877Le document en format XML
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<term>Betacoronavirus (chemistry)</term>
<term>Betacoronavirus (immunology)</term>
<term>Betacoronavirus (metabolism)</term>
<term>Betacoronavirus (ultrastructure)</term>
<term>Cross Reactions</term>
<term>Cryoelectron Microscopy</term>
<term>Image Processing, Computer-Assisted</term>
<term>Models, Molecular</term>
<term>Peptidyl-Dipeptidase A (metabolism)</term>
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<term>Protein Multimerization</term>
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<term>SARS Virus (chemistry)</term>
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<term>Spike Glycoprotein, Coronavirus (chemistry)</term>
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<term>Spike Glycoprotein, Coronavirus (ultrastructure)</term>
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<term>Spike Glycoprotein, Coronavirus</term>
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<term>Image Processing, Computer-Assisted</term>
<term>Models, Molecular</term>
<term>Protein Binding</term>
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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<Abstract><AbstractText>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.</AbstractText>
<CopyrightInformation>Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</CopyrightInformation>
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