Monitoring lectin interactions with carbohydrates.

Methods Mol Biol

Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM), UMR7255 CNRS-Aix Marseille Université, Institut de Microbiologie de la Méditerranée, 31 Chemin Joseph Aiguier, Marseille Cédex 20, 13402, France,

Published: March 2015

AI Article Synopsis

  • Protein-carbohydrate interactions play a crucial role in the initial stages of infection, particularly with the pathogen Pseudomonas aeruginosa, which produces proteins that specifically bind to host glycan epitopes.
  • Experimental methods for studying these interactions have been adapted from those used in protein-protein or protein-ligand studies.
  • Various techniques are outlined for assessing lectin activity, identifying sugar specificity, measuring binding affinity along with thermodynamic and kinetic parameters, and crystallizing lectin-carbohydrate complexes for detailed structural analysis.

Article Abstract

Protein-carbohydrate interactions are often involved in the first step of infection and Pseudomonas aeruginosa produces several proteins that are able to bind specifically to glycan epitopes present on host epithelia. The experimental approaches for studying protein-carbohydrate interaction have been inspired, with some adaptations, from those commonly used for protein-protein or protein-ligand interactions. A range of methods are described herein for detecting lectin activity, screening for monosaccharide or oligosaccharide specificity, determining the affinity of binding together with thermodynamics and kinetics parameters, and producing crystal of lectin-carbohydrate complexes for further structural studies.

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Source
http://dx.doi.org/10.1007/978-1-4939-0473-0_32DOI Listing

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