Receptors for carbohydrate ligands including heparin on the cell surface of Leishmania and other trypanosomatids.

By employing neoglycoproteins (NGP) and glycosaminoglycans, the detection of endogenous glycoligand-binding sites has become possible. Monitoring specific binding of 11 of these sugar receptor-specific tools, 13 trypanosomatids of monogenetic genera Blastocrithidia, Crithidia, Herpetomonas, and Leptomonas and digenetic genera Endotrypanum, Leishmania, and Sauroleishmania were analysed by agglutination and fluorescence assays. NGP showed agglutination reactions only with the digenetic but not with the monogenetic species. Sensitive flow cytofluorimetric investigations revealed that the apparently different reactivity to NGP is due to a pronounced quantitative difference in expression of binding sites between mono- and digenetic flagellates. Moreover, flow cytofluorimetry was used to demonstrate the occurrence of receptor sites for heparin on the cell surfaces of all trypanosomatids. An indication for a correlation of the binding capacity for the NGP N-acetyl-beta-D-glucosamine and heparin to differences in the pathogenicity of parasites was observed for Leishmania donovani as well as Leishmania enriettii. Infective populations of these species contained a significantly higher number of cells which had bound N-acetyl-beta-D-glucosamine and heparin than noninfective (long-term in vitro-cultured) populations. The results of the present report additionally support the hypothesis that lectin-carbohydrate interactions with neutral sugar moieties and heparin or heparin-like molecules participate in the interactions between trypanosomatids and host (cells), and that the detected binding sites for carbohydrates and heparin may thus be referred to as potential virulence factors.