A glycolipid from Trypanosoma brucei related to the variant surface glycoprotein membrane anchor

Mol Biochem Parasitol. 1989 Oct;36(3):263-70. doi: 10.1016/0166-6851(89)90174-6.

Abstract

The variant surface glycoprotein (VSG) of Trypanosoma brucei is covalently linked to a phosphatidylinositol-containing glycolipid which serves as a membrane anchor. We previously identified a molecule, glycolipid A, which appears to be a biosynthetic precursor to the anchor [9]. In this paper we describe a related molecule, glycolipid C, which is similar to glycolipid A but which is more hydrophobic. Chromatographic analyses indicate that the polar head groups in glycolipids A and C are similar or identical. Both glycolipids contain phosphatidylinositol, but the inositol in glycolipid C is modified by a hydrophobic moiety. Since treatment of glycolipid C with mild alkali results in partial conversion to a molecule chromatographically identical to glycolipid A, it is likely that glycolipid C has an alkali-sensitive hydrophobic group, such as a fatty acid, linked to its inositol moiety.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Chromatography, Thin Layer
  • Glycolipids / analysis*
  • Glycolipids / isolation & purification
  • Membrane Glycoproteins / analysis*
  • Phosphatidylinositols
  • Solubility
  • Trypanosoma brucei brucei / analysis*

Substances

  • Glycolipids
  • Membrane Glycoproteins
  • Phosphatidylinositols