Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.
Identifieur interne : 000347 ( PubMed/Curation ); précédent : 000346; suivant : 000348Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.
Auteurs : Young-Jun Park [États-Unis] ; Alexandra C. Walls [États-Unis] ; Zhaoqian Wang [États-Unis] ; Maximillian M. Sauer [États-Unis] ; Wentao Li [Pays-Bas] ; M Alejandra Tortorici [États-Unis] ; Berend-Jan Bosch [Pays-Bas] ; Frank Dimaio [États-Unis] ; David Veesler [États-Unis]Source :
- Nature structural & molecular biology [ 1545-9985 ] ; 2019.
Descripteurs français
- KwdFr :
- Acides sialiques (), Acides sialiques (métabolisme), Cartographie d'interactions entre protéines, Conformation des glucides, Conformation des protéines, Coronavirus du syndrome respiratoire du Moyen-Orient (), Cryomicroscopie électronique, Dipeptidyl peptidase 4 (), Dipeptidyl peptidase 4 (métabolisme), Dipeptidyl peptidase 4 (ultrastructure), Domaines protéiques, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (métabolisme), Glycoprotéine de spicule des coronavirus (ultrastructure), Humains, Hémagglutination virale, Liaison aux protéines, Modèles moléculaires, Relation structure-activité, Sites de fixation.
- MESH :
- métabolisme : Acides sialiques, Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus.
- ultrastructure : Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus.
- Acides sialiques, Cartographie d'interactions entre protéines, Conformation des glucides, Conformation des protéines, Coronavirus du syndrome respiratoire du Moyen-Orient, Cryomicroscopie électronique, Dipeptidyl peptidase 4, Domaines protéiques, Glycoprotéine de spicule des coronavirus, Humains, Hémagglutination virale, Liaison aux protéines, Modèles moléculaires, Relation structure-activité, Sites de fixation.
English descriptors
- KwdEn :
- Binding Sites, Carbohydrate Conformation, Cryoelectron Microscopy, Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (metabolism), Dipeptidyl Peptidase 4 (ultrastructure), Hemagglutination, Viral, Humans, Middle East Respiratory Syndrome Coronavirus (chemistry), Models, Molecular, Protein Binding, Protein Conformation, Protein Domains, Protein Interaction Mapping, Sialic Acids (chemistry), Sialic Acids (metabolism), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (metabolism), Spike Glycoprotein, Coronavirus (ultrastructure), Structure-Activity Relationship.
- MESH :
- chemical , chemistry : Dipeptidyl Peptidase 4, Sialic Acids, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Dipeptidyl Peptidase 4, Sialic Acids, Spike Glycoprotein, Coronavirus.
- chemical , ultrastructure : Dipeptidyl Peptidase 4, Spike Glycoprotein, Coronavirus.
- chemistry : Middle East Respiratory Syndrome Coronavirus.
- Binding Sites, Carbohydrate Conformation, Cryoelectron Microscopy, Hemagglutination, Viral, Humans, Models, Molecular, Protein Binding, Protein Conformation, Protein Domains, Protein Interaction Mapping, Structure-Activity Relationship.
Abstract
The Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe and often lethal respiratory illness in humans, and no vaccines or specific treatments are available. Infections are initiated via binding of the MERS-CoV spike (S) glycoprotein to sialosides and dipeptidyl-peptidase 4 (the attachment and entry receptors, respectively). To understand MERS-CoV engagement of sialylated receptors, we determined the cryo-EM structures of S in complex with 5-N-acetyl neuraminic acid, 5-N-glycolyl neuraminic acid, sialyl-LewisX, α2,3-sialyl-N-acetyl-lactosamine and α2,6-sialyl-N-acetyl-lactosamine at 2.7-3.0 Å resolution. We show that recognition occurs via a conserved groove that is essential for MERS-CoV S-mediated attachment to sialosides and entry into human airway epithelial cells. Our data illuminate MERS-CoV S sialoside specificity and suggest that selectivity for α2,3-linked over α2,6-linked receptors results from enhanced interactions with the former class of oligosaccharides. This study provides a structural framework explaining MERS-CoV attachment to sialoside receptors and identifies a site of potential vulnerability to inhibitors of viral entry.
DOI: 10.1038/s41594-019-0334-7
PubMed: 31792450
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<term>Dipeptidyl Peptidase 4 (chemistry)</term>
<term>Dipeptidyl Peptidase 4 (metabolism)</term>
<term>Dipeptidyl Peptidase 4 (ultrastructure)</term>
<term>Hemagglutination, Viral</term>
<term>Humans</term>
<term>Middle East Respiratory Syndrome Coronavirus (chemistry)</term>
<term>Models, Molecular</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Protein Domains</term>
<term>Protein Interaction Mapping</term>
<term>Sialic Acids (chemistry)</term>
<term>Sialic Acids (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus (chemistry)</term>
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<term>Acides sialiques (métabolisme)</term>
<term>Cartographie d'interactions entre protéines</term>
<term>Conformation des glucides</term>
<term>Conformation des protéines</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient ()</term>
<term>Cryomicroscopie électronique</term>
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<term>Domaines protéiques</term>
<term>Glycoprotéine de spicule des coronavirus ()</term>
<term>Glycoprotéine de spicule des coronavirus (métabolisme)</term>
<term>Glycoprotéine de spicule des coronavirus (ultrastructure)</term>
<term>Humains</term>
<term>Hémagglutination virale</term>
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<term>Modèles moléculaires</term>
<term>Relation structure-activité</term>
<term>Sites de fixation</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dipeptidyl Peptidase 4</term>
<term>Sialic Acids</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
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<term>Carbohydrate Conformation</term>
<term>Cryoelectron Microscopy</term>
<term>Hemagglutination, Viral</term>
<term>Humans</term>
<term>Models, Molecular</term>
<term>Protein Binding</term>
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<front><div type="abstract" xml:lang="en">The Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe and often lethal respiratory illness in humans, and no vaccines or specific treatments are available. Infections are initiated via binding of the MERS-CoV spike (S) glycoprotein to sialosides and dipeptidyl-peptidase 4 (the attachment and entry receptors, respectively). To understand MERS-CoV engagement of sialylated receptors, we determined the cryo-EM structures of S in complex with 5-N-acetyl neuraminic acid, 5-N-glycolyl neuraminic acid, sialyl-Lewis<sup>X</sup>
, α2,3-sialyl-N-acetyl-lactosamine and α2,6-sialyl-N-acetyl-lactosamine at 2.7-3.0 Å resolution. We show that recognition occurs via a conserved groove that is essential for MERS-CoV S-mediated attachment to sialosides and entry into human airway epithelial cells. Our data illuminate MERS-CoV S sialoside specificity and suggest that selectivity for α2,3-linked over α2,6-linked receptors results from enhanced interactions with the former class of oligosaccharides. This study provides a structural framework explaining MERS-CoV attachment to sialoside receptors and identifies a site of potential vulnerability to inhibitors of viral entry.</div>
</front>
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<ArticleTitle>Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.</ArticleTitle>
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<Abstract><AbstractText>The Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe and often lethal respiratory illness in humans, and no vaccines or specific treatments are available. Infections are initiated via binding of the MERS-CoV spike (S) glycoprotein to sialosides and dipeptidyl-peptidase 4 (the attachment and entry receptors, respectively). To understand MERS-CoV engagement of sialylated receptors, we determined the cryo-EM structures of S in complex with 5-N-acetyl neuraminic acid, 5-N-glycolyl neuraminic acid, sialyl-Lewis<sup>X</sup>
, α2,3-sialyl-N-acetyl-lactosamine and α2,6-sialyl-N-acetyl-lactosamine at 2.7-3.0 Å resolution. We show that recognition occurs via a conserved groove that is essential for MERS-CoV S-mediated attachment to sialosides and entry into human airway epithelial cells. Our data illuminate MERS-CoV S sialoside specificity and suggest that selectivity for α2,3-linked over α2,6-linked receptors results from enhanced interactions with the former class of oligosaccharides. This study provides a structural framework explaining MERS-CoV attachment to sialoside receptors and identifies a site of potential vulnerability to inhibitors of viral entry.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Park</LastName>
<ForeName>Young-Jun</ForeName>
<Initials>YJ</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Walls</LastName>
<ForeName>Alexandra C</ForeName>
<Initials>AC</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Zhaoqian</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Sauer</LastName>
<ForeName>Maximillian M</ForeName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Wentao</ForeName>
<Initials>W</Initials>
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<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Institut Pasteur, Unité de Virologie Structurale, Paris, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>CNRS UMR 3569, Unité de Virologie Structurale, Paris, France.</Affiliation>
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<ForeName>Berend-Jan</ForeName>
<Initials>BJ</Initials>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>DiMaio</LastName>
<ForeName>Frank</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA, USA.</Affiliation>
</AffiliationInfo>
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<ForeName>David</ForeName>
<Initials>D</Initials>
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<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA, USA. dveesler@uw.edu.</Affiliation>
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