Lectin Binding by Trypanosoma equiperdum

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Abstract
Agglutination studies with 6 plant lectins indicated that the unaltered surface coat of T. equiperdum isolated from rat blood lacks the carbohydrate molecules preferentially bound by these proteins. Trypsin, Pronase, chymopapain or papain treatments exposed the binding sites for concanavalin A [Con-A] and the phytohemagglutinins M and P and trypsinized cells were attached to Con-A immobilized on agarose beads. Lipolytic, amylytic and other proteolytic enzymes or other agents did not reduce or induce lectin agglutination and wheat germ, Anti A and Anti H lectins did not clump the trypanosomes under any of the conditions employed. Carbohydrate residues resembling D-mannose or n-acetyl-D-galactosamine are within the surface coat of T. equiperdum or on the cell membrane underneath it. The results are contrasted with lectin induced agglutination of other parasite species and mammalian cells.