National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
120553
United States
Citation
Journal: Nat Struct Mol Biol / Year: 2019 Title: Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors. Authors: Young-Jun Park / Alexandra C Walls / Zhaoqian Wang / Maximillian M Sauer / Wentao Li / M Alejandra Tortorici / Berend-Jan Bosch / Frank DiMaio / David Veesler / 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 ...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.
History
Deposition
Aug 1, 2019
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Header (metadata) release
Dec 11, 2019
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Map release
Dec 11, 2019
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Update
Dec 2, 2020
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Current status
Dec 2, 2020
Processing site: RCSB / Status: Released
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Surface view with section colored by density value
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