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High affinity binding strategies for bacterial lectins interacting with eukaryotic carbohydrates
Author(s) -
Imberty Anne,
Michaela Wimmerova,
Mitchell Edward P
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a58-c
Subject(s) - biochemistry , avidity , lectin , ralstonia solanacearum , chemistry , glycan , isothermal titration calorimetry , biology , bacteria , glycoprotein , genetics , antibody , immunology
Lectin‐carbohydrate interactions are generally characterised by a low affinity for monovalent ligands, a drawback balanced by multivalency that provides high avidity for substrates with several potential ligands available, such as complex glycans or cell surfaces. In general, a millimolar affinity is observed for lectin binding to monosaccharides. Better affinity is obtained for longer ligand, i.e. oligosaccharides, and the interactions are typified by a favourable enthalpy term, due to the high number of hydrogen bonds, that is offset by an unfavourable entropy contribution. Recent interest in bacterial lectins involved in pathogenesis and host recognition has been accompanied by thermodynamic characterisation that demonstrated much higher affinity than that observed for plant or animal lectins. Calcium–dependent lectins from opportunistic pathogens Pseudomonas aeruginosa, Chromobacterium violaceaum and Ralstonia solanacearum all display sub‐micromolar range affinity towards their carbohydrate ligands. We used combined titration microcalorimetry and x‐ray crystallography approaches to decipher the thermodynamical and structural basis for high affinity binding of bacterial lectins to host carbohydrates. Research funded by CNRS, Association “Vaindre la Mucoviscidose” and Mizutani foundation for Glycosciences