Structural requirements for the binding of glycopeptides to immobilized Vicia faba (FAVA) lectin

Abstract The structural requirements for the binding of oligosaccharides and glycopeptides to immobilized Vicia faba agglutinin were investigated, and its carbohydrate specificity was compared with the specificities of the α- d -mannose-binding lectins concanavalin A, Lens culinaris agglutinin, and Pisum sativum agglutinin. Immobilized Vicia faba agglutinin can interact only with biantennary glycopeptides possessing an α- l -fucosyl group attached to the l -asparagine-linked 2-acetamido-2-deoxy-β- d -glucopyranosyl residue. An l -asparagine residue is essential for high affinity-binding to Vicia faba agglutinin-Sepharose. In addition, the enzymic exposure of a (nonreducing) terminal α- d -mannosyl group enhances the interaction of the glycopeptide with immobilized Vicia faba agglutinin. This sugar-binding specificity of immobilized Vicia faba agglutinin is similar to that of immobilized Pisum sativum agglutinin.