The properties and function of the glycosylphosphatidylinositol-phospholipase C in Trypanosoma brucei

Mol Biochem Parasitol. 1998 Mar 1;91(1):153-64. doi: 10.1016/s0166-6851(97)00190-4.


The purpose of this review is to consider recent results obtained concerning the properties and function of the glycosylphosphatidylinositol-phospholipase C (GPI-PLC) in Trypanosoma brucei. A mutagenesis study that provides evidence that the GPI-PLC is more closely related to bacterial PI-PLCs than previously realised is described. The variant specific glycoprotein (VSG), which dominates the surface of the mammalian stages of the trypanosome, is almost certainly the major substrate of the GPI-PLC. The hydrolysis of the GPI-anchor of the VSG under stress conditions and hypotonic lysis is well established. To investigate whether this hydrolysis of the GPI-anchor plays any role during the life cycle a GPI-PLC null mutant has been made. The phenotype indicates that the gene is non-essential, but its absence alters the course of infection in mice.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Gene Deletion
  • Glycosylphosphatidylinositol Diacylglycerol-Lyase
  • Glycosylphosphatidylinositols / metabolism
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Substrate Specificity
  • Trypanosoma brucei brucei / enzymology*
  • Trypanosoma brucei brucei / genetics
  • Trypanosomiasis, African / immunology
  • Trypanosomiasis, African / parasitology*
  • Type C Phospholipases / chemistry
  • Type C Phospholipases / genetics
  • Type C Phospholipases / metabolism*
  • Variant Surface Glycoproteins, Trypanosoma / metabolism


  • Glycosylphosphatidylinositols
  • Variant Surface Glycoproteins, Trypanosoma
  • Type C Phospholipases
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Glycosylphosphatidylinositol Diacylglycerol-Lyase