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Glycopeptide mimetics recapitulate high-mannose-type oligosaccharide binding and function.

Sabrina Lusvarghi1, Rodolfo Ghirlando, Chi-Huey Wong

  • 1Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892 (USA).

Angewandte Chemie (International Ed. in English)
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Summary

Designing glycopeptide mimetics revealed how mannose valency and spacing influence interactions with griffithsin (GRFT). This provides insights into high-mannose-type glycan (HMTG) mediated viral inhibition.

Keywords:
antiviral agentscarbohydratesglycansmultivalencyoligomerization

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Area of Science:

  • Carbohydrate Chemistry
  • Structural Biology
  • Virology

Background:

  • High-mannose-type glycans (HMTGs) on viral spike proteins are key targets for neutralization.
  • Multivalency is crucial for carbohydrate-binding proteins to achieve high avidity and potent inhibition.

Purpose of the Study:

  • To define chemical determinants controlling multivalent interactions of HMTGs.
  • To design and characterize glycopeptide mimetics of HMTGs.

Main Methods:

  • NMR spectroscopy
  • Surface Plasmon Resonance (SPR)
  • Analytical ultracentrifugation
  • Microcalorimetry

Main Results:

  • Designed glycopeptide HMTG mimetics with varied mannose valency and spacing.
  • Glycopeptides recapitulated specificity and kinetics of griffithsin (GRFT) binding to Man9 GlcNAc2 Asn and a synthetic nonamannoside.
  • Mannose spacing and valency determined face-to-face vs. intermolecular binding modes with GRFT.
  • Face-to-face interactions showed higher affinity, while intermolecular interactions were longer-lived.

Conclusions:

  • Mannose valency and spacing are critical determinants of glycopeptide binding modes.
  • Distinct binding modes (face-to-face vs. intermolecular) have different affinity and kinetic profiles.
  • Findings offer insights into mechanisms of glycan-mediated viral inhibition.