Effects of neuraminidase on lectin binding sites in photoreceptor cells of monkey retina.

Binding of sugar-specific lectins to the monkey retina was investigated with particular reference to the effects of pretreatment with neuraminidase on the photoreceptor cells. Neuraminidase-treated or untreated retinal sections were examined with a fluorescence microscope after incubation with the following fluorescein-labeled lectins: peanut agglutinin (PNA), wheat germ agglutinin (WGA), Ricinus communis agglutinin-1 (RCA-1) and Dolichos biflorus agglutinin (DBA). In the neuraminidase-untreated tissue, PNA, which is specific for D-galactose beta 1----3 N-acetyl-D-galactosamine (Gal beta 1----3GalNAc), was bound preferentially to the cones, and after treatment of sections with neuraminidase, PNA could bind to both cones and rods. WGA, which is specific for sialic acid and N-acetyl-D-glucosamine, was strongly bound to the rods but moderately to the cones without neuraminidase pretreatment, whereas neuraminidase-treated sections showed a weak binding. RCA-1, which is specific for D-galactose, showed patchy fluorescence on the basal and distal portions of the outer segments of the cones and rods, whereas neuraminidase-treated sections had uniform fluorescence throughout the tissues. DBA, which is specific for N-acetyl-D-galactosamine, did not bind to either cones or rods before and after neuraminidase treatment. These results suggest that there is a difference in the carbohydrate chains of glycoconjugates in the cones and rods: in the cones Gal beta 1----3GalNAc may be the terminal sugar as recognized by PNA, whereas in the rods this sugar is contained in the carbohydrate chain but masked by terminal sialyl residues so that those glycoconjugates are inaccessible to PNA without neuraminidase treatment.