Interaction of Trypanosoma cruzi with macrophages: effect of previous incubation of the parasites or the host cells with lectins.
The effect of incubation with lectins of the macrophages or two evolutive stages of Trypanosoma cruzi (noninfective epimastigotes and infective trypomastigotes) on the ingestion of the parasites by mouse peritoneal macrophages was studied. Lectins which bind to residues of mannose (Lens culinaris, LCA), N-acetyl-D-glucosamine or N-acetylneuraminic acid (Triticum vulgaris, WGA), beta-D-galactose (Ricinus communis, RCA), N-acetyl-D-galactosamine (Phaseolus vulgaris, PHA; Dolichos biflorus, DBA; and Wistaria floribunda, WFA), fucose (Lotus tetragonolobus, LTA), and N-acetylneuraminic acid (Limulus polyphemus, LPA) were used. By lectin blockage we concluded that, alpha-D-mannose-like, beta-D-galactose and N-acetyl-D-galactosamine (PHA, reagent) residues, located on the macrophage's surface are required for both epi- and trypomastigote uptake, while N-acetylneuraminic acid and fucose residues, impede trypomastigote ingestion but do not interfere with epimastigote interiorization. Macrophages' N-acetyl-D-glucosamine residues are required for epimastigote uptake. On the other hand, from the T. cruzi surface, mannose residues prevent ingestion of epi- and trypomastigotes. Galactose residues participate in endocytosis of trypomastigotes, but hinder epimastigote interiorization. Exposed N-acetyl-D-glucosamine residues are required for uptake of the two evolutive forms. N-acetylneuraminic acid residues on the trypomastigote membrane prevent their endocytosis by macrophages. These results together with those reported previously showing the effect of monosaccharides on the T. cruzi-macrophage interaction, indicate that (a) sugar residues located on the parasite and on macrophage surface play some role in the process of recognition of T. cruzi, (b) different macrophage carbohydrate-containing receptors are involved in the recognition of epimastigotes and trypomastigotes forms of T. cruzi, (c) N-acetylneuraminic acid residues located on the surface of trypomastigotes or macrophages impede the interaction of the parasite with these host cells, and suggest that (d) sugar-binding proteins located on the macrophage surface participate in the recognition of beta-D-galactose and N-acetyl-D-galactosamine residues located on the surface of trypomastigotes and exposed after blockage or splitting off of N-acetylneuraminic acid residues. Some lectins which bind to macrophages and block the ingestion of parasites did not interfere with their adhesion.
D000116:Acetylgalactosamine / Q000502:physiology; D000117:Acetylglucosamine / Q000502:physiology; D000818:Animals; D060829:Arthropod Proteins; D002241:Carbohydrates / Q000502:physiology*; D014355:Chagas Disease / Q000469:parasitology; D004705:Endocytosis; D005643:Fucose / Q000502:physiology; D005690:Galactose / Q000502:physiology; D005947:Glucose / Q000502:physiology; D006801:Humans; D037102:Lectins / Q000494:pharmacology*; D008264:Macrophages / Q000502:physiology*; D008358:Mannose / Q000502:physiology; D051379:Mice; D010835:Phytohemagglutinins / Q000494:pharmacology; D037121:Plant Lectins; D034781:Receptors, N-Acetylglucosamine; D012794:Sialic Acids / Q000502:physiology; D014349:Trypanosoma cruzi / Q000502:physiology*; D014909:Wheat Germ Agglutinins
D060829:Arthropod Proteins; D002241:Carbohydrates; D037102:Lectins; D010835:Phytohemagglutinins; D037121:Plant Lectins; D034781:Receptors, N-Acetylglucosamine; C017707:Ricinus communis agglutinin-1; D012794:Sialic Acids; D014909:Wheat Germ Agglutinins; C033619:lentil lectin; C040129:wisteria lectin; D005643:Fucose; D005947:Glucose; D000116:Acetylgalactosamine; D008358:Mannose; D000117:Acetylglucosamine; D005690:Galactose