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J. Biol. Chem., Vol. 267, Issue 17, 11721-11728, 06, 1992
S Tomavo, JF Dubremetz and RT Schwarz
Four major glycolipids were extracted from Toxoplasma gondii tachyzoites
which were metabolically labeled with tritiated glucosamine, mannose,
palmitic and myristic acid, ethanolamine, and inositol. Judging from their
sensitivity to a set of enzymatic and chemical tests, these glycolipids
share the following properties with the glycolipid moiety of the
glycosylphosphatidylinositol anchor (GPI anchor) of the major surface
protein, P30, of T. gondii: 1) a nonacetylated glucosamine-inositol
phosphate linkage; 2) sensitivity toward phosphatidylinositol-specific
phospholipase C and nitrous acid; 3) identity of HF-dephosphorylated GPI
glycan backbone between three glycolipids and the HF-dephosphorylated core
glycan of the GPI anchor of the major surface protein P30; 4) the presence
of a linear core glycan structure blocked by an ethanolamine phosphate
residue(s). Taken together with the nature of radiolabeled precursors
incorporated into these glycolipids, the data indicate that these GPIs are
involved in the biosynthesis of the GPI-membrane anchors of T. gondii.
A family of glycolipids from Toxoplasma gondii. Identification of candidate glycolipid precursor(s) for Toxoplasma gondii glycosylphosphatidylinositol membrane anchors
Zentrum fur Hygiene und Medizinische Mikrobiologie, Philipps- Universitat Marburg, Germany.
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