MersV1, PubMed, Checkpoint, bibRecord, 000366

Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.

Identifieur interne : 000366 ( PubMed/Checkpoint ); précédent : 000365; suivant : 000367

Structures 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.

RBID : pubmed:31792450

Descripteurs français

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-Lewis^X, 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

Affiliations:

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Le document en format XML

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<term>Carbohydrate Conformation</term>
<term>Cryoelectron Microscopy</term>
<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>
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<term>Protein Interaction Mapping</term>
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<term>Sialic Acids (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus (chemistry)</term>
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<term>Spike Glycoprotein, Coronavirus (ultrastructure)</term>
<term>Structure-Activity Relationship</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>
<term>Dipeptidyl peptidase 4 ()</term>
<term>Dipeptidyl peptidase 4 (métabolisme)</term>
<term>Dipeptidyl peptidase 4 (ultrastructure)</term>
<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>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Relation structure-activité</term>
<term>Sites de fixation</term>
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<term>Sialic Acids</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
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<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides sialiques</term>
<term>Dipeptidyl peptidase 4</term>
<term>Glycoprotéine de spicule des coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Dipeptidyl peptidase 4</term>
<term>Glycoprotéine de spicule des coronavirus</term>
</keywords>
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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>
<term>Protein Conformation</term>
<term>Protein Domains</term>
<term>Protein Interaction Mapping</term>
<term>Structure-Activity Relationship</term>
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<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>Glycoprotéine de spicule des coronavirus</term>
<term>Humains</term>
<term>Hémagglutination virale</term>
<term>Liaison aux protéines</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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<DateCompleted><Year>2020</Year>
<Month>02</Month>
<Day>12</Day>
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<Month>03</Month>
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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>
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<ForeName>Young-Jun</ForeName>
<Initials>YJ</Initials>
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</AffiliationInfo>
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<ForeName>Alexandra C</ForeName>
<Initials>AC</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA, USA.</Affiliation>
</AffiliationInfo>
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<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>
<Initials>MM</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Wentao</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, the Netherlands.</Affiliation>
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Serveur d'exploration MERS

Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.

Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.

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