STRUCTURAL CHARACTERIZATION OF THE MAJOR GLYCOSYLPHOSPHATIDYLINOSITOL MEMBRANE-ANCHORED GLYCOPROTEIN FROM EPIMASTIGOTE FORMS OF TRYPANOSOMA-CRUZI Y-STRAIN
- Previato, J. O.
- Jones, C.
- Xavier, M. T.
- Wait, R.
- Travassos, Luiz Rodolpho
- Parodi, A. J.
- Mendonca-Previato, L.
DOIAbstract
We have investigated the structure of the glycosylphosphatidylinositol (GPI) anchor and the O-linked glycan chains of the 40/45-kDa glycoprotein from the cell surface of the protozoan parasite Trypanosoma cruzi, This glycoconjugate is the major acceptor for sialic acid transferred by trans sialidase of T. cruzi Y-strain, epimastigote form. The GPI anchor was liberated by treatment with hot alkali, and the phosphoinositol-oligosaccharide moiety was characterized and shown to have the following structure.[GRAPHICS]STRUCTURE 1Unusually the glucosamine was 6-O-substituted with 2-aminoethylphosphonate, and 2-aminoethylphosphonate was also present on the third mannose residue distal to glucosamine, partially replacing the ethanolamine phosphate, ...
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