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TitleStructural basis for human coronavirus attachment to sialic acid receptors.
Journal, issue, pagesNat Struct Mol Biol, Vol. 26, Issue 6, Page 481-489, Year 2019
Publish dateJun 3, 2019
AuthorsM Alejandra Tortorici / Alexandra C Walls / Yifei Lang / Chunyan Wang / Zeshi Li / Danielle Koerhuis / Geert-Jan Boons / Berend-Jan Bosch / Félix A Rey / Raoul J de Groot / David Veesler /
PubMed AbstractCoronaviruses cause respiratory tract infections in humans and outbreaks of deadly pneumonia worldwide. Infections are initiated by the transmembrane spike (S) glycoprotein, which binds to host ...Coronaviruses cause respiratory tract infections in humans and outbreaks of deadly pneumonia worldwide. Infections are initiated by the transmembrane spike (S) glycoprotein, which binds to host receptors and fuses the viral and cellular membranes. To understand the molecular basis of coronavirus attachment to oligosaccharide receptors, we determined cryo-EM structures of coronavirus OC43 S glycoprotein trimer in isolation and in complex with a 9-O-acetylated sialic acid. We show that the ligand binds with fast kinetics to a surface-exposed groove and that interactions at the identified site are essential for S-mediated viral entry into host cells, but free monosaccharide does not trigger fusogenic conformational changes. The receptor-interacting site is conserved in all coronavirus S glycoproteins that engage 9-O-acetyl-sialogycans, with an architecture similar to those of the ligand-binding pockets of coronavirus hemagglutinin esterases and influenza virus C/D hemagglutinin-esterase fusion glycoproteins. Our results demonstrate these viruses evolved similar strategies to engage sialoglycans at the surface of target cells.
External linksNat Struct Mol Biol / PubMed:31160783 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 2.9 Å
Structure data

0557

6nzk

EMDB-0557, PDB-6nzk:
Structural basis for human coronavirus attachment to sialic acid receptors
Method: EM (single particle) / Resolution: 2.8 Å

20070

6ohw

EMDB-20070, PDB-6ohw:
Structural basis for human coronavirus attachment to sialic acid receptors. Apo-HCoV-OC43 S
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MJJ:
methyl 9-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid

ChemComp-HOH:
WATER

Source
  • Betacoronavirus
  • human coronavirus oc43
KeywordsVIRAL PROTEIN / Coronavirus spike glycoprotein / sialic acid / HCoV-OC43 / fusion protein

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