Characterization of carbohydrate binding proteins in Trypanosoma cruzi.
Abstract
Trypanosoma cruzi is an obligatory intracellular protozoan parasite that causes Chagas' disease in humans and invades a great variety of mammalian cells. The nature of the ligand(s) and receptor components in both T. cruzi and target cells remains controversial, although it seems to involve an interaction with oligosaccharides. In an attempt to identify possible ligands on the parasite, we have searched for the presence of carbohydrate binding proteins (CBPs) in T. cruzi. By fluorescence-activated cell sorter analysis using a panel of fluoresceinated glyco- and neoglycopeptides with well characterized glycans, the presence of at least two different CBPs was identified on the surface of T. cruzi epimastigotes and trypomastigotes. The specificity of binding of the two CBPs seems to be mediated by galactose and mannose residues. The mannose- and galactose-mediated CBPs from epimastigotes and trypomastigotes were purified to homogeneity by affinity chromatography on immobilized thyroglobulin and identified as 60-70-kDa glycoproteins. Purified CBPs were able to specifically bind with high affinity to murine and human macrophages as well as other cell types susceptible to infection by T. cruzi but not to fat or neuronal cells. This b...Continue Reading
References
Involvement of beta 1 integrins in the binding and entry of Trypanosoma cruzi into human macrophages
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