Effects of neuraminidase on lectin binding by wild-type and ricin-resistant strains of hamster fibroblasts.

The nature of cell surface receptors for ricin on wild-type and ricin-resistant variants of baby hamster kidney fibroblasts has been studied. Neuraminidase stimulated ricin binding threefold by wild-type cells, and increased their susceptibility to ricin toxicity as measured by inhibition of [3H]leucine uptake (LD30 fell from 5.0 to 0.5 microgram/mL). Basal ricin binding by ricin-resistant variants (10-300% that of wild type) was also stimulated (2- to 17-fold) by neuraminidase in all seven clonal strains examined; susceptibility to ricin was greatly increased by neuraminidase in these variants. Neuraminidase did not affect the binding of concanavalin A by wild type or a ricin-resistant variant, but decreased the binding of wheat-germ agglutinin by 90% in both cell types. The trivial binding of peanut agglutinin by wild type and a ricin-resistant variant was markedly enhanced (14- to 22-fold) by neuraminidase. Neither collagenase (50 U/mL) nor Pronase (0.0001%) affected ricin binding by wild type or a ricin-resistant variant. These data suggest the existence of "exposed" and "cryptic" oligosaccharide receptors for ricin on the cell membrane glycoproteins of baby hamster kidney fibroblasts. The cryptic ricin receptors probably include at least the sequence D-galactosyl-beta-(1 replaced by 3)-N-acetylhexosamine substituted by sialic acid residues. Exposed and cryptic ricin receptors appear to be different and under separate genetic control.