Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi Epimastigotes. |
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| Authors: | R M de Lederkremer C Lima M I Ramirez M A Ferguson S W Homans J Thomas-Oates |
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| Affiliation: | Departamento de Quimica Organica, Facultad de Ciencas Exactas y Naturales, Universidad de Buenos Aires, Argentina. |
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| Abstract: | The lipopeptidophosphoglycan is the major cell surface glycoconjugate of the epimastigote forms of the parasitic protozoan Trypanosoma cruzi. A detailed partial structure for this molecule has been reported (Previato, J. O., Gorin, P. A. J., Mazurek, M., Xavier, M. T., Fournet, B., Wieruszesk, J. M., and Mendonca-Previato, L. (1990) J. Biol. Chem. 265, 2518-2526). In this study, we complete the primary structure assignments and describe the microheterogeneity found in the lipopeptidophosphoglycan glycan, using a combination of 1H and 31P NMR, fast atom bombardment mass spectrometry, methylation linkage analysis, and exoglycosidase sequencing. The lipopeptidophosphoglycan is a glycosylated inositol-phosphoceramide with striking homology to glycosylphosphatidylinositol membrane anchors found attached to a wide variety of plasma membrane proteins throughout the eukaryotes. |
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