Binding of sulfatide to concanavalin A and Lens culinaris agglutinin

概要

論文の詳細を見る
Lectins, carbohydrate binding proteins of non-immune origin, are characterized by a high degree of specificity in binding to some saccharides in preference to others. Some lectins are reported to interact with sulfated glycosaminoglycans, but little is known about an interaction between lectins and sulfatide. Here, we examined the binding of sulfatide to leguminous plant lectins, such as Lens culinaris agglutinin (LCA), concanavalin A (Con A), peanut agglutinin, soybean agglutinin, Solanum tuberosum agglutinin, Ulex europaeus agglutinin, and Bauhinia purpurea agglutinin. A solid phase binding assay using horse radish peroxidase-labeled lectins showed that LCA and Con A could bind to sulfatide coated on microtiter plates, but failed to bind to galactosylceramide. The binding of these lectins to sulfatide was inhibited in the presence of excess amounts of either methyl α-D-mannopyranoside or D-glucose, whereas it was not affected by D-galactose. Furthermore, both Con A and LCA bound to sulfatide which was incorporated into lipid vesicles and the binding was inhibited by addition of methyl α-D-mannopyranoside. These results suggest that Con A and LCA have a binding site of sulfatide whose affinity is affected by the specific binding of saccharides.
2009-02-27