title: Assessment of weak sugar-binding ability using lectin tetramer and membrane-based glycans.
abstract: To consider biological significance of glycosylation of proteins, it is necessary to evaluate the importance of sugar-recognition processes mediated by lectins. Though the interaction between sugars and proteins, especially animal lectins, is quite weak with K d approximately 10(-4) M, cellular and molecular recognitions mediated via sugar-protein interaction increase their avidity by 1-3 orders of magnitude by the self-association of both receptors and their ligands on cell surfaces. To assess the weak interaction between lectins and their sugar ligands, we established lectin tetramer binding to cell surface glycans using flow cytometry. This strategy is highly sensitive, and useful to determine whether or not a putative lectin domain may have sugar-binding ability.
authors.affiliation: Laboratory of Molecular Medicine, Department of Integrated Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba, 277-8562, Japan, yamamoto@k.u-tokyo.ac.jp.
authors.forename: Kazuo
authors.initials: K
authors.lastname: Yamamoto
mesh_terms: D019921:Biotinylation; D002462:Cell Membrane / Q000378:metabolism*; D005434:Flow Cytometry / Q000379:methods*; D006367:HeLa Cells; D006801:Humans; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism*; D010799:Phycoerythrin / Q000737:chemistry; D011134:Polysaccharides / Q000378:metabolism*; D011485:Protein Binding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D012995:Solubility
chemical_list: D037102:Lectins; D011134:Polysaccharides; D010799:Phycoerythrin