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

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-LewisX, 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.
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Submitted on : Saturday, April 18, 2020 - 3:42:21 AM
Last modification on : Friday, April 24, 2020 - 1:47:31 AM

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Young-Jun Park, Alexandra Walls, Zhaoqian Wang, Maximillian Sauer, Wentao Li, et al.. Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors. Nature Structural and Molecular Biology, Nature Publishing Group, 2019, 26 (12), pp.1151-1157. ⟨10.1038/s41594-019-0334-7⟩. ⟨pasteur-02546517⟩

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