Human tandem-repeat-type galectins bind bacterial non-βGal polysaccharides

• Published in: Glycoconjugate journal 2014, Vol.31 (1), p.7-12
• Main Authors: Knirel, Yu. A., Gabius, H.-J., Blixt, O., Rapoport, E. M., Khasbiullina, N. R., Shilova, N. V., Bovin, N. V.
• Format: Article
• Language: English
• Subjects: Binding Sites; Biochemistry; Biomedical and Life Sciences; Epitopes - metabolism; Escherichia coli; Galactosides - chemistry; Galectins - chemistry; Galectins - metabolism; Glycoarray Section; Humans; Life Sciences; Pathology; Polysaccharides, Bacterial - chemistry; Polysaccharides, Bacterial - metabolism; Protein Binding; Repetitive Sequences, Amino Acid; Rhamnose - chemistry
• ISSN: 0282-0080; 1573-4986
• DOI: 10.1007/s10719-013-9497-3

Galectins are multifunctional effectors, for example acting as regulators of cell growth via protein-glycan interactions. The observation of capacity to kill bacteria for two tandem-repeat-type galectins, which target histo-blood epitopes toward this end (Stowell et al . Nat. Med. 16:295–301, 2010 ), prompted us to establish an array with bacterial polysaccharides. We addressed the question whether sugar determinants other than β-galactosides may be docking sites, using human galectins-4, -8, and -9. Positive controls with histo-blood group ABH-epitopes and the E. coli 086 polysaccharide ascertained the suitability of the set-up. Significant signal generation, depending on type of galectin and polysacchride, was obtained. Presence of cognate β-galactoside-related epitopes within a polysaccharide chain or its branch will not automatically establish binding properties, and structural constellations lacking galactosides, like rhamnan, were found to be active. These data establish the array as valuable screening tool, giving direction to further functional and structural studies.