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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
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What contributes to an effective mannose recognition domain?

Christoph P Sager1, Deniz Eriş1, Martin Smieško1

  • 1Department of Pharmaceutical Sciences, University of Basel, Klingelbergstrasse 50, CH-4056 Basel, Switzerland.

Beilstein Journal of Organic Chemistry
|December 21, 2017
PubMed
Summary

Nature uses specific binding strategies to enhance carbohydrate-lectin interactions, overcoming low affinity through optimized hydrogen bonds and binding site structures. Bacterial lectins like FimH show improved affinity via deep binding sites and catch-bond mechanisms.

Keywords:
carbohydrate–lectin interactionsdesolvation penaltydielectric constantmultivalencypre-organization

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Carbohydrate-lectin interactions typically exhibit high specificity but low affinity due to desolvation costs.
  • Nature employs strategies to enhance these interactions, particularly in innate immunity and bacterial adhesion.

Purpose of the Study:

  • To analyze mannose-binding sites in C-type lectins and bacterial adhesins.
  • To understand characteristics that enable successful carbohydrate recognition.

Main Methods:

  • Comparative analysis of mannose-binding sites in six C-type lectins and three bacterial adhesins.
  • Investigated hydrogen bonding and binding site geometry.

Main Results:

  • High desolvation costs are compensated by the number and quality of hydrogen bonds.
  • Bacterial lectin FimH exhibits a deep binding site, improving off-rate compared to mammalian lectins.
  • Bacterial strategies like catch-bonds and multivalency further enhance affinity.

Conclusions:

  • Optimized hydrogen bonding and binding site architecture are crucial for carbohydrate-lectin affinity.
  • Bacterial lectins utilize unique structural features and mechanisms to achieve high affinity interactions.
  • Understanding these natural strategies offers potential for developing carbohydrate-based therapeutics.