Structural Basis of the Preferential Binding for Globo-Series Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I

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Authors	BLANCHARD Bertrand NURISSO Alessandra HOLLWILLE Emilie TETAUD Cecile WIELLS Joele POKORNÁ Martina WIMMEROVÁ Michaela VARROTTE Annabelle IMBERTY Anne
Year of publication	2008
Type	Article in Periodical
Magazine / Source	Journal of Molecular Biology
MU Faculty or unit	Faculty of Science
Citation
Field	Biophysics
Keywords	pseudomonas aeruginosa; lectin; molecular modeling; structure;glycosphinglipid; oligosaccharides
Description	The opportunistic pathogen Pseudomonas aeruginosa contains several carbohydrate-binding proteins, among which is the P. aeruginosa lectin I (PA-IL), which displays affinity for a-galactosylated glycans. Glycan arrays were screened and demonstrated stronger binding of PA-IL toward aGal1-4bGal-terminating structures and weaker binding to aGal1-3bGal ones in order to determine which human glycoconjugates could play a role in the carbohydrate-mediated adhesion of the bacteria. This was confirmed in vivo by testing the binding of the lectin to Burkitt lymphoma cells that present large amounts of globotriaosylceramide antigen Gb3/CD77/Pk. Trisaccharide moieties of Gb3 and isoglobotriaosylceramide were tested by titration microcalorimetry, and both displayed similar affinity to PA-IL in solution.
Related projects:	Proteins in metabolism and interaction of organisms with the environment