Lectins are carbohydrate-binding proteins that interact with specific sugars or glycoconjugates and mediate several biological activities. Bacterial lectins are involved in host recognition, bioiilm formation, tissue adhesion and virulence. Pseudomonas aeruginosa and Burkholderia cenocepacia are opportunistic pathogens responsible for lung infections that are life-threatening for cystic fibrosis patients and immuno-compromised individuals. Both bacteria contain several calcium-dependant lectins that demonstrate high affinity for diverse oligosaccharides that are present on human tissues. We used combined titration microcalorimetry, x-ray crystallography and molecular modeling approaches to decipher the thermodynamical and structural basis for high affinity binding of bacterial lectins to host carbohydrates [1,2].
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