Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding.
Identifieur interne : 000E57 ( Main/Exploration ); précédent : 000E56; suivant : 000E58Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding.
Auteurs : Miao Gui [République populaire de Chine] ; Wenfei Song [République populaire de Chine] ; Haixia Zhou [République populaire de Chine] ; Jingwei Xu [République populaire de Chine] ; Silian Chen [République populaire de Chine] ; Ye Xiang [République populaire de Chine] ; Xinquan Wang [République populaire de Chine]Source :
- Cell research [ 1748-7838 ] ; 2017.
Descripteurs français
- KwdFr :
- Anticorps neutralisants (métabolisme), Conformation des protéines, Cryomicroscopie électronique, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (ultrastructure), Humains, Liaison aux protéines, Modèles biologiques, Modèles moléculaires, Multimérisation de protéines, Récepteurs de surface cellulaire (métabolisme), Virus du SRAS (ultrastructure).
- MESH :
English descriptors
- KwdEn :
- Antibodies, Neutralizing (metabolism), Cryoelectron Microscopy, Humans, Models, Biological, Models, Molecular, Protein Binding, Protein Conformation, Protein Multimerization, Receptors, Cell Surface (metabolism), SARS Virus (ultrastructure), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (ultrastructure).
- MESH :
- chemical , chemistry : Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Antibodies, Neutralizing, Receptors, Cell Surface.
- ultrastructure : SARS Virus, Spike Glycoprotein, Coronavirus.
- Cryoelectron Microscopy, Humans, Models, Biological, Models, Molecular, Protein Binding, Protein Conformation, Protein Multimerization.
Abstract
The global outbreak of SARS in 2002-2003 was caused by the infection of a new human coronavirus SARS-CoV. The infection of SARS-CoV is mediated mainly through the viral surface glycoproteins, which consist of S1 and S2 subunits and form trimer spikes on the envelope of the virions. Here we report the ectodomain structures of the SARS-CoV surface spike trimer in different conformational states determined by single-particle cryo-electron microscopy. The conformation 1 determined at 4.3 Å resolution is three-fold symmetric and has all the three receptor-binding C-terminal domain 1 (CTD1s) of the S1 subunits in "down" positions. The binding of the "down" CTD1s to the SARS-CoV receptor ACE2 is not possible due to steric clashes, suggesting that the conformation 1 represents a receptor-binding inactive state. Conformations 2-4 determined at 7.3, 5.7 and 6.8 Å resolutions are all asymmetric, in which one RBD rotates away from the "down" position by different angles to an "up" position. The "up" CTD1 exposes the receptor-binding site for ACE2 engagement, suggesting that the conformations 2-4 represent a receptor-binding active state. This conformational change is also required for the binding of SARS-CoV neutralizing antibodies targeting the CTD1. This phenomenon could be extended to other betacoronaviruses utilizing CTD1 of the S1 subunit for receptor binding, which provides new insights into the intermediate states of coronavirus pre-fusion spike trimer during infection.
DOI: 10.1038/cr.2016.152
PubMed: 28008928
Affiliations:
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type="city">Pékin</settlement></placeName></affiliation></author></analytic><series><title level="j">Cell research</title><idno type="eISSN">1748-7838</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Neutralizing (metabolism)</term><term>Cryoelectron Microscopy</term><term>Humans</term><term>Models, Biological</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Receptors, Cell Surface (metabolism)</term><term>SARS Virus (ultrastructure)</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (ultrastructure)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps neutralisants (métabolisme)</term><term>Conformation des protéines</term><term>Cryomicroscopie électronique</term><term>Glycoprotéine 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xml:lang="en"><term>Cryoelectron Microscopy</term><term>Humans</term><term>Models, Biological</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Multimerization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cryomicroscopie électronique</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles biologiques</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The global outbreak of SARS in 2002-2003 was caused by the infection of a new human coronavirus SARS-CoV. The infection of SARS-CoV is mediated mainly through the viral surface glycoproteins, which consist of S1 and S2 subunits and form trimer spikes on the envelope of the virions. Here we report the ectodomain structures of the SARS-CoV surface spike trimer in different conformational states determined by single-particle cryo-electron microscopy. The conformation 1 determined at 4.3 Å resolution is three-fold symmetric and has all the three receptor-binding C-terminal domain 1 (CTD1s) of the S1 subunits in "down" positions. The binding of the "down" CTD1s to the SARS-CoV receptor ACE2 is not possible due to steric clashes, suggesting that the conformation 1 represents a receptor-binding inactive state. Conformations 2-4 determined at 7.3, 5.7 and 6.8 Å resolutions are all asymmetric, in which one RBD rotates away from the "down" position by different angles to an "up" position. The "up" CTD1 exposes the receptor-binding site for ACE2 engagement, suggesting that the conformations 2-4 represent a receptor-binding active state. This conformational change is also required for the binding of SARS-CoV neutralizing antibodies targeting the CTD1. This phenomenon could be extended to other betacoronaviruses utilizing CTD1 of the S1 subunit for receptor binding, which provides new insights into the intermediate states of coronavirus pre-fusion spike trimer during infection.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Gui, Miao" sort="Gui, Miao" uniqKey="Gui M" first="Miao" last="Gui">Miao Gui</name></noRegion><name sortKey="Chen, Silian" sort="Chen, Silian" uniqKey="Chen S" first="Silian" last="Chen">Silian Chen</name><name sortKey="Song, Wenfei" sort="Song, Wenfei" uniqKey="Song W" first="Wenfei" last="Song">Wenfei Song</name><name sortKey="Wang, Xinquan" sort="Wang, Xinquan" uniqKey="Wang X" first="Xinquan" last="Wang">Xinquan Wang</name><name sortKey="Xiang, Ye" sort="Xiang, Ye" uniqKey="Xiang Y" first="Ye" last="Xiang">Ye Xiang</name><name sortKey="Xu, Jingwei" sort="Xu, Jingwei" uniqKey="Xu J" first="Jingwei" last="Xu">Jingwei Xu</name><name sortKey="Zhou, Haixia" sort="Zhou, Haixia" uniqKey="Zhou H" first="Haixia" last="Zhou">Haixia Zhou</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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