Structural basis for human coronavirus attachment to sialic acid receptors

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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

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M Alejandra Tortorici1,2,3, Alexandra C Walls1, Yifei Lang4

  • 1Department of Biochemistry, University of Washington, Seattle, WA, USA.

Nature Structural & Molecular Biology
|June 5, 2019
PubMed

Insights

Coronaviruses use their spike (S) glycoprotein to attach to host cells. Researchers determined the structure of the OC43 S glycoprotein bound to 9-O-acetylated sialic acid, revealing key interactions for viral entry.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Coronaviruses are a significant cause of human respiratory infections and pneumonia outbreaks.
  • Viral entry into host cells is initiated by the spike (S) glycoprotein mediating receptor binding and membrane fusion.

Purpose of the Study:

  • To elucidate the molecular mechanisms of coronavirus attachment to oligosaccharide receptors.
  • To determine the cryo-electron microscopy (cryo-EM) structures of the OC43 S glycoprotein in isolation and complex with 9-O-acetylated sialic acid.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine high-resolution structures.
  • Structural analysis of the OC43 S glycoprotein trimer.
  • Investigation of the complex between the S glycoprotein and 9-O-acetylated sialic acid.

Main Results:

  • The cryo-EM structure revealed the binding of 9-O-acetylated sialic acid to a surface-exposed groove on the OC43 S glycoprotein.
  • Ligand binding exhibited fast kinetics and was essential for S-mediated viral entry, though free monosaccharide did not induce fusogenic changes.
  • The identified receptor-interacting site is conserved across coronaviruses utilizing 9-O-acetyl-sialoglycans and shares architectural similarities with hemagglutinin-esterase fusion glycoproteins.

Conclusions:

  • The study provides detailed structural insights into coronavirus attachment to sialic acid receptors.
  • The findings highlight conserved strategies among viruses for engaging sialoglycans on target cell surfaces.
  • Understanding these interactions is crucial for developing antiviral strategies against coronavirus infections.

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