Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.
Identifieur interne : 000D00 ( Main/Exploration ); précédent : 000C99; suivant : 000D01Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.
Auteurs : Wenfei Song [République populaire de Chine] ; Miao Gui [République populaire de Chine] ; Xinquan Wang [République populaire de Chine] ; Ye Xiang [République populaire de Chine]Source :
- PLoS pathogens [ 1553-7374 ] ; 2018.
Descripteurs français
- KwdFr :
- Cryomicroscopie électronique, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (métabolisme), Liaison aux protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Peptidyl-Dipeptidase A (), Peptidyl-Dipeptidase A (métabolisme), Pénétration virale, Récepteurs viraux (), Récepteurs viraux (métabolisme), Structure quaternaire des protéines, Syndrome respiratoire aigu sévère (virologie), Virus du SRAS ().
- MESH :
- métabolisme : Glycoprotéine de spicule des coronavirus, Peptidyl-Dipeptidase A, Récepteurs viraux.
- virologie : Syndrome respiratoire aigu sévère.
- Cryomicroscopie électronique, Glycoprotéine de spicule des coronavirus, Liaison aux protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Peptidyl-Dipeptidase A, Pénétration virale, Récepteurs viraux, Structure quaternaire des protéines, Virus du SRAS.
English descriptors
- KwdEn :
- Cryoelectron Microscopy, Models, Molecular, Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (metabolism), Protein Binding, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Quaternary, Receptors, Virus (chemistry), Receptors, Virus (metabolism), SARS Virus (chemistry), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (metabolism), Virus Internalization.
- MESH :
- chemical , chemistry : Peptidyl-Dipeptidase A, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Peptidyl-Dipeptidase A, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemistry : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Cryoelectron Microscopy, Models, Molecular, Protein Binding, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Quaternary, Virus Internalization.
Abstract
The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.
DOI: 10.1371/journal.ppat.1007236
PubMed: 30102747
Affiliations:
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Song</name><affiliation wicri:level="3"><nlm:affiliation>The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, Beijing, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, Beijing</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Gui, Miao" sort="Gui, Miao" uniqKey="Gui M" first="Miao" last="Gui">Miao Gui</name><affiliation wicri:level="3"><nlm:affiliation>Center for Infectious Disease Research, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Beijing 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(chemistry)</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (chemistry)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cryomicroscopie électronique</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Multimérisation de protéines</term><term>Peptidyl-Dipeptidase A ()</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Pénétration virale</term><term>Récepteurs viraux ()</term><term>Récepteurs viraux (métabolisme)</term><term>Structure quaternaire des protéines</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Virus du SRAS 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Microscopy</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Protein Multimerization</term><term>Protein Structure, Quaternary</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cryomicroscopie électronique</term><term>Glycoprotéine de spicule des coronavirus</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Multimérisation de protéines</term><term>Peptidyl-Dipeptidase A</term><term>Pénétration virale</term><term>Récepteurs viraux</term><term>Structure quaternaire des protéines</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.</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="Song, Wenfei" sort="Song, Wenfei" uniqKey="Song W" first="Wenfei" last="Song">Wenfei Song</name></noRegion><name sortKey="Gui, Miao" sort="Gui, Miao" uniqKey="Gui M" first="Miao" last="Gui">Miao Gui</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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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