Glycosyl-sn-1,2-dimyristylphosphatidylinositol is covalently linked to Trypanosoma brucei variant surface glycoprotein.

作者: M A Ferguson , M G Low , G A Cross

DOI: 10.1016/S0021-9258(17)38603-9

关键词:

摘要: The COOH terminus of the externally disposed variant surface glycoprotein (VSG) eukaryotic pathogenic protozoan Trypanosoma brucei strain 427 MITat 1.4 (117) is covalently linked to a novel phosphatidylinositol-containing glycolipid. This conclusion supported by analysis products nitrous acid deamination or Staphylococcus aureus phosphatidylinositol-specific phospholipase C treatment purified membrane-form VSG. Lysis trypanosomes accompanied release soluble VSG, catalyzed activation an endogenous C. only apparent difference between VSG and removal sn-1,2-dimyristylglycerol. COOH-terminal glycopeptide derived Pronase digestion was characterized chemical modification with alkaline phosphatase. results are consistent single non-N-acetylated glucosamine residue being reducing oligosaccharide in glycosidic linkage myo-inositol monophosphate that probably 1,2-cyclic monophosphate. A partial structure for moiety presented. represents new type post-translational protein membrane anchor. We discuss relevance this observations have been made other proteins.

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