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

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature structural & molecular biology - 02 Dec 2019

Park YJ, Walls AC, Wang Z, Sauer MM, Li W, Tortorici MA, Bosch BJ, DiMaio F, Veesler D

Link to Pubmed [PMID] – 31792450

Nat. Struct. Mol. Biol. 2019 12;26(12):1151-1157

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.

https://www.ncbi.nlm.nih.gov/pubmed/31792450