Characterization and isolation of concanavalin A binding sites from the epidermis of S. mansoni.

Using concanavalin A labeled with tritium and fluorescein isothiocyanate we studied the binding properties of this plant lectin to adult paired schistosomes. Using concanavalin A coupled to a sepharose column we attempted to isolate and characterize concanavalin A binding molecules from the epidermis of adult schistosomes. Our results indicate the presence of specific concanavalin A binding sites on the surface of adult Schistosoma mansoni. A significant percentage of the concanavalin A was specifically bound and showed characteristics similar to that identical in other concanavalin A binding tissues. The parasite's concanavalin A binding sites appear to be 2 or 3 high molecular weight glycoproteins. There is some indication that glycoproteins associated with the worm's epidermis function as enzyme(s). The immunological significance of these glycoproteins has not been determined.