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Structure paper

TitleStructures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.
Journal, issue, pagesNat Struct Mol Biol, Vol. 26, Issue 12, Page 1151-1157, Year 2019
Publish dateDec 2, 2019
AuthorsYoung-Jun Park / Alexandra C Walls / Zhaoqian Wang / Maximillian M Sauer / Wentao Li / M Alejandra Tortorici / Berend-Jan Bosch / Frank DiMaio / David Veesler /
PubMed AbstractThe 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 ...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, 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.
External linksNat Struct Mol Biol / PubMed:31792450 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 3.0 Å
Structure data

20542

6q04

EMDB-20542, PDB-6q04:
MERS-CoV S structure in complex with 5-N-acetyl neuraminic acid
Method: EM (single particle) / Resolution: 2.5 Å

20543

6q05

EMDB-20543, PDB-6q05:
MERS-CoV S structure in complex with sialyl-lewisX
Method: EM (single particle) / Resolution: 2.8 Å

20544

6q06

EMDB-20544, PDB-6q06:
MERS-CoV S structure in complex with 2,3-sialyl-N-acetyl-lactosamine
Method: EM (single particle) / Resolution: 2.7 Å

20545

6q07

EMDB-20545, PDB-6q07:
MERS-CoV S structure in complex with 2,6-sialyl-N-acetyl-lactosamine
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-20829:
MERS-CoV S structure in complex with 5-N-glycolyl neuraminic acid
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-FOL:
FOLIC ACID / Folate

ChemComp-SIA:
N-acetyl-alpha-neuraminic acid / Sialic acid

ChemComp-HOH:
WATER / Water

Source
  • Middle East respiratory syndrome-related coronavirus
  • human betacoronavirus 2c emc/2012
KeywordsVIRAL PROTEIN / Coronavirus / spike glycoprotein / MERS-CoV / membrane fusion / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID

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