Park_2019_Nat.Struct.Mol.Biol_26_1151

Reference

Title : Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors - Park_2019_Nat.Struct.Mol.Biol_26_1151
Author(s) : Park YJ , Walls AC , Wang Z , Sauer MM , Li W , Tortorici MA , Bosch BJ , DiMaio F , Veesler D
Ref : Nat Struct Mol Biol , 26 :1151 , 2019
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), alpha2,3-sialyl-N-acetyl-lactosamine and alpha2,6-sialyl-N-acetyl-lactosamine at 2.7-3.0 A 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 alpha2,3-linked over alpha2,6-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.

PubMedSearch : Park_2019_Nat.Struct.Mol.Biol_26_1151
PubMedID: 31792450

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Citations formats

Park YJ, Walls AC, Wang Z, Sauer MM, Li W, Tortorici MA, Bosch BJ, DiMaio F, Veesler D (2019)
Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
Nat Struct Mol Biol 26 :1151

Park YJ, Walls AC, Wang Z, Sauer MM, Li W, Tortorici MA, Bosch BJ, DiMaio F, Veesler D (2019)
Nat Struct Mol Biol 26 :1151