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Pathogen-sugar interactions revealed by universal saturation transfer analysis.

Charles J Buchanan^1,2,3, Ben Gaunt¹, Peter J Harrison^4,5

¹Rosalind Franklin Institute, Harwell Science and Innovation Campus, Oxford OX11 0FA, UK.

Science (New York, N.Y.)

|June 23, 2022

Summary

This summary is machine-generated.

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike proteins bind to sialoside sugars using an "end-on" approach, as revealed by universal saturation transfer analysis (uSTA). This interaction, involving the N-terminal domain (NTD), may influence viral virulence and zoonosis.

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Area of Science:

Virology
Structural Biology
Biochemistry

Background:

Pathogens frequently utilize host cell-surface glycans for infection.
Analyzing glycan-protein interactions is challenging due to overlapping signals and experimental limitations.

Purpose of the Study:

To develop and apply an automated method for quantifying protein-ligand interactions.
To investigate the binding mode of SARS-CoV-2 spike proteins to glycan ligands.

Main Methods:

Utilized universal saturation transfer analysis (uSTA), an automated nuclear magnetic resonance spectroscopy workflow.
Integrated uSTA with computational modeling and cryo-electron microscopy (cryo-EM).

Main Results:

Demonstrated that SARS-CoV-2 spike trimers bind sialoside sugars in an "end-on" orientation.
Identified the spike N-terminal domain (NTD) as crucial for this sugar binding.
Correlated NTD mutations in variants of concern with abolished sugar binding.

Conclusions:

The end-on binding of sialoside sugars by the SARS-CoV-2 spike NTD is a key finding.
This interaction implicates a specific sialylated glycan motif in the human lung as potentially relevant to SARS-CoV-2 virulence and zoonosis.
Findings provide insights into SARS-CoV-2 pathogenesis and host-pathogen interactions.