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Carbohydrate-Lectin Interactions: An Unexpected Contribution to Affinity.

Giulio Navarra1, Pascal Zihlmann1, Roman P Jakob2

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Chembiochem : a European Journal of Chemical Biology
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Summary
This summary is machine-generated.

Blocking uropathogenic E. coli’s PapG-II adhesin can prevent kidney infections. Elongating the natural ligand increased binding affinity, offering a novel therapeutic approach beyond antibiotics.

Keywords:
PapGX-ray diffractionantiadhesivepyelonephritisthermodynamics

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Area of Science:

  • Microbiology
  • Structural Biology
  • Drug Discovery

Background:

  • Uropathogenic E. coli (UPEC) causes kidney infections using PapG-II adhesin.
  • PapG-II expression on pili correlates with pyelonephritis, a severe condition.
  • Targeting PapG-II offers an alternative to antibiotics for UPEC infections.

Purpose of the Study:

  • To identify potent PapG-II antagonists.
  • To investigate the mechanism behind increased ligand-lectin affinity.

Main Methods:

  • Synthesis of tetrasaccharide and hexasaccharide ligands.
  • Isothermal Titration Calorimetry (ITC) to measure binding affinity.

Main Results:

  • Hexasaccharide ligand showed increased binding affinity for PapG-II compared to tetrasaccharide.
  • Increased affinity is attributed to partial desolvation of non-contact regions.
  • This desolvation perturbs outer hydration layers, enhancing binding.

Conclusions:

  • Ligand elongation, even in non-contact regions, can enhance binding affinity.
  • Desolvation of nonbinding ligand regions is a key mechanism for modulating carbohydrate-protein interactions.
  • This finding provides a general strategy for designing carbohydrate-based inhibitors.