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-Structure paper
タイトル | Structural basis for human coronavirus attachment to sialic acid receptors. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 26, Issue 6, Page 481-489, Year 2019 |
掲載日 | 2019年6月3日 |
![]() | M Alejandra Tortorici / Alexandra C Walls / Yifei Lang / Chunyan Wang / Zeshi Li / Danielle Koerhuis / Geert-Jan Boons / Berend-Jan Bosch / Félix A Rey / Raoul J de Groot / David Veesler / ![]() ![]() ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 2.8 - 2.9 Å |
構造データ | EMDB-0557, PDB-6nzk: EMDB-20070, PDB-6ohw: |
化合物 | ![]() ChemComp-NAG: ![]() ChemComp-MJJ: ![]() ChemComp-HOH: |
由来 |
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![]() | VIRAL PROTEIN / Coronavirus spike glycoprotein / sialic acid / HCoV-OC43 / fusion protein |