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© Gail Rozen-Gagnon, Christine Schmitt,
Cells infected with Chikungunya (CHIK) virus.
Publication : Nature structural & molecular biology

Structural basis for human coronavirus attachment to sialic acid receptors

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature structural & molecular biology - 03 Jun 2019

Tortorici MA, Walls AC, Lang Y, Wang C, Li Z, Koerhuis D, Boons GJ, Bosch BJ, Rey FA, de Groot RJ, Veesler D

Link to Pubmed [PMID] – 31160783

Nat. Struct. Mol. Biol. 2019 Jun;26(6):481-489

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.

https://www.ncbi.nlm.nih.gov/pubmed/31160783