Lectin binding by trypanosoma equiperdum.
Agglutination studies with 6 plant lectins indicated that the unaltered surface coat of Trypanosoma equiperdum isolated from rat blood lacks the carbohydrate molecules preferentially bound by these proteins. However, trypsin, pronase, chymopapain, or papain treatments exposed the binding sites for Concanavalin A and the phytohemagglutinins M and P and trypsinized cells were attached to Concanavalin 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 therefore within the surface coat of T. equiperdum or on the cell membrane underneath it. The results are contrasted with the lectin induced agglutination of other parasite species and mammalian cells.
D000371:Agglutination / Q000187:drug effects; D000818:Animals; D002917:Chymopapain / Q000494:pharmacology; D003208:Concanavalin A / Q000494:pharmacology; D037102:Lectins / Q000494:pharmacology*; D008297:Male; D008358:Mannose / Q000494:pharmacology; D010206:Papain / Q000494:pharmacology; D011402:Pronase / Q000494:pharmacology; D051381:Rats; D014345:Trypanosoma / Q000187:drug effects / Q000276:immunology*; D014357:Trypsin / Q000494:pharmacology
D037102:Lectins; D003208:Concanavalin A; D014357:Trypsin; D010206:Papain; D002917:Chymopapain; D011402:Pronase; D008358:Mannose