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Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes

  • Rosa M. de Lederkremer
  • , Carlos Lima
  • , Maria I. Ramirez
  • , Michael A. J. Ferguson
  • , Steve W. Homans
  • , Jane Thomas-Oates

    Research output: Contribution to journalArticlepeer-review

    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 membrane anchors found attached to a wide variety of plasma membrane proteins throughout the eukaryotes.

    Original languageEnglish
    Pages (from-to)23670-23675
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume266
    Issue number35
    Publication statusPublished - 15 Dec 1991

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