Ultrastructural localization of lectin-binding sites on the surface of the guinea pig conjunctival epithelium.

The cell-surface binding sites of two lectins, concanavalin A (Con A) and wheat-germ agglutinin (WGA) in the guinea pig conjunctiva were investigated at the ultrastructural level by means of pre-embedding staining of the tissue with lectin-colloidal gold complexes. Wheat-germ agglutinin, which recognizes N-acetylglucosamine and sialic acid residues, showed prominent and fairly uniform binding to the microvilli. The binding was markedly increased in the vicinity of the goblet cells, indicating that the same carbohydrate ligands were also present in the mucus. In contrast, no binding of concanavalin A, which recognizes mannose and N-glucose, was observed. The results suggest the presence of sialic acid and galactose as the constituent carbohydrates of glycoconjugates in the surface membrane of conjunctival epithelial cells as well as in the mucus produced by the goblet cells.