Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi Epimastigotes.

  1. R M de Lederkremer,
  2. C Lima,
  3. M I Ramirez,
  4. M A Ferguson,
  5. S W Homans and
  6. J Thomas-Oates
  1. Departamento de Quimica Organica, Facultad de Ciencas Exactas y Naturales, Universidad de Buenos Aires, Argentina.

    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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