Ultrastructural localization of lectin receptors in the monkey retinal photoreceptors and pigment epithelium: application of lectin-gold complexes on thin sections.

The cell surface and intracellular binding sites of two lectins, wheat germ agglutinin (WGA) and Ricinus communis agglutinin-1 (RCA-1), in the monkey retina were investigated at the ultrastructural level by means of post-embedding staining of Lowicryl K4M-embedded specimens with lectin-colloidal gold complexes. Effects of pretreatment with neuraminidase were also studied. The techniques enabled us to detect lectin binding sites in the various intracellular compartments of photoreceptor cells, retinal pigment epithelium (RPE), and interphotoreceptor matrices. Wheat germ agglutinin, which recognizes N-acetylglucosamine and sialic-acid residues, showed a prominent and uniform binding to the disc membranes of rod outer segments (ROS), rod connecting cilia, interphotoreceptor matrices, and RPE microvilli. The intensity of these binding sites was markedly reduced when thin sections were pretreated with neuraminidase, except the labeling of ROS disc membranes. Cones were labeled sparsely. The staining of phagosomes in the RPE cytoplasm did not change after neuraminidase digestion. RCA-1, which recognizes galactose residues, revealed a moderate binding to the ROS disc membranes, with a noticeably greater intensity of binding to the basal region of ROS disc membranes. With neuraminidase treatment heavier binding with RCA-1 occurred in interphotoreceptor matrices, connecting cilia and RPE microvilli, whereas there was no significant alteration in binding to the ROS disc membranes. Phagosomes in the RPE were also labeled with this lectin. The results suggest the presence of sialic acid and galactose as the constituent carbohydrates of glycoconjugates in the interphotoreceptor matrices and RPE microvilli.