Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin

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Authors	LAMEIGNERE Emilie SHIAO Tze Chieh ROY Rene WIMMEROVÁ Michaela DUBREUIL Fréderic VARROT Annabelle IMBERTY Anne
Year of publication	2010
Type	Article in Periodical
Magazine / Source	Glycobiology
MU Faculty or unit	Faculty of Science
Citation
Doi	https://doi.org/10.1093/glycob/cwp151
Field	Biophysics
Keywords	bacterial lectin;Burkholderia cenocepacia;mannose;oligosaccharides
Description	The disaccharides and the trisaccharide,Man1-3(Man1-6)Man were tested by titration microcalorimetry in order to evaluate their affinity for BC2L-A in solution and to characterize the thermodynamics of the binding. Oligomannose analogs presenting two mannoside residues separated by either flexible or rigid spacer where also tested.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Biomolecular centre Design of Carbohydrates and Glycomimetics as Antibacterial and Antiviral Drugs Lectins from human pathogens - structure, function, engineering