Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Identifieur interne : 000749 ( 2020/Analysis ); précédent : 000748; suivant : 000750Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Auteurs : Daniel Wrapp [États-Unis] ; Nianshuang Wang [États-Unis] ; Kizzmekia S. Corbett [États-Unis] ; Jory A. Goldsmith [États-Unis] ; Ching-Lin Hsieh [États-Unis] ; Olubukola Abiona [États-Unis] ; Barney S. Graham [États-Unis] ; Jason S. Mclellan [États-Unis]Source :
- Science (New York, N.y.) [ 0036-8075 ] ; 2020.
Descripteurs français
- KwdFr :
- Anticorps antiviraux (immunologie), Anticorps monoclonaux (immunologie), Conformation des protéines, Cryomicroscopie électronique, Domaines protéiques, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (immunologie), Glycoprotéine de spicule des coronavirus (métabolisme), Glycoprotéine de spicule des coronavirus (ultrastructure), Liaison aux protéines, Modèles moléculaires, Multimérisation de protéines, Peptidyl-Dipeptidase A (métabolisme), Réactions croisées, Récepteurs viraux (métabolisme), Traitement d'image par ordinateur, Virus du SRAS (), Virus du SRAS (immunologie), Virus du SRAS (ultrastructure).
- MESH :
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Glycoprotéine de spicule des coronavirus, Virus du SRAS.
- métabolisme : Glycoprotéine de spicule des coronavirus, Peptidyl-Dipeptidase A, Récepteurs viraux.
- Conformation des protéines, Cryomicroscopie électronique, Domaines protéiques, Glycoprotéine de spicule des coronavirus, Liaison aux protéines, Modèles moléculaires, Multimérisation de protéines, Réactions croisées, Traitement d'image par ordinateur, Virus du SRAS.
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 World Health Organization has declared the outbreak of a novel coronavirus
(2019-nCoV) to be a public health emergency of international concern. The virus binds to
host cells through its trimeric spike glycoprotein, making this protein a key target for
potential therapies and diagnostics. Wrapp
Url:
DOI: 10.1126/science.abb2507
PubMed: 32075877
PubMed Central: 7164637
Affiliations:
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PMC:7164637Le document en format XML
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<term>Antibodies, Viral (immunology)</term>
<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>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Protein Domains</term>
<term>Protein Multimerization</term>
<term>Receptors, Virus (metabolism)</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (immunology)</term>
<term>SARS Virus (ultrastructure)</term>
<term>Spike Glycoprotein, Coronavirus (chemistry)</term>
<term>Spike Glycoprotein, Coronavirus (immunology)</term>
<term>Spike Glycoprotein, Coronavirus (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus (ultrastructure)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps antiviraux (immunologie)</term>
<term>Anticorps monoclonaux (immunologie)</term>
<term>Conformation des protéines</term>
<term>Cryomicroscopie électronique</term>
<term>Domaines protéiques</term>
<term>Glycoprotéine de spicule des coronavirus ()</term>
<term>Glycoprotéine de spicule des coronavirus (immunologie)</term>
<term>Glycoprotéine de spicule des coronavirus (métabolisme)</term>
<term>Glycoprotéine de spicule des coronavirus (ultrastructure)</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Multimérisation de protéines</term>
<term>Peptidyl-Dipeptidase A (métabolisme)</term>
<term>Réactions croisées</term>
<term>Récepteurs viraux (métabolisme)</term>
<term>Traitement d'image par ordinateur</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (immunologie)</term>
<term>Virus du SRAS (ultrastructure)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term>
</keywords>
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<term>Spike Glycoprotein, Coronavirus</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Betacoronavirus</term>
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Betacoronavirus</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Receptors, Virus</term>
<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Récepteurs viraux</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Betacoronavirus</term>
<term>SARS Virus</term>
<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cross Reactions</term>
<term>Cryoelectron Microscopy</term>
<term>Image Processing, Computer-Assisted</term>
<term>Models, Molecular</term>
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<term>Protein Domains</term>
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<front><div type="abstract" xml:lang="en"><title>Structure of the nCoV trimeric spike</title>
<p>The World Health Organization has declared the outbreak of a novel coronavirus
(2019-nCoV) to be a public health emergency of international concern. The virus binds to
host cells through its trimeric spike glycoprotein, making this protein a key target for
potential therapies and diagnostics. Wrapp <italic>et al.</italic>
determined a
3.5-angstrom-resolution structure of the 2019-nCoV trimeric spike protein by
cryo–electron microscopy. Using biophysical assays, the authors show that this
protein binds at least 10 times more tightly than the corresponding spike protein of
severe acute respiratory syndrome (SARS)–CoV to their common host cell receptor.
They also tested three antibodies known to bind to the SARS-CoV spike protein but did not
detect binding to the 2019-nCoV spike protein. These studies provide valuable information
to guide the development of medical counter-measures for 2019-nCoV.</p>
<p><italic>Science</italic>
, this issue p. <ext-link ext-link-type="doi" xlink:href="10.1126/science.abb2507">1260</ext-link>
</p>
</div>
</front>
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