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

Jessica L. Krakow, Tamara L. Doering, Wayne J. Masterson, Gerald W. Hart, Paul T. Englund

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

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.

Original languageEnglish
Pages (from-to)263-270
Number of pages8
JournalMolecular and Biochemical Parasitology
Volume36
Issue number3
DOIs
StatePublished - Oct 1989
Externally publishedYes

Keywords

  • Glycolipid
  • Glycosyl phosphatidylinositol
  • Membrane anchor
  • Trypanosome
  • Variant surface glycoprotein

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