M. Carrington et al., THE PROPERTIES AND FUNCTION OF THE GLYCOSYLPHOSPHATIDYLINOSITOL-PHOSPHOLIPASE-C IN TRYPANOSOMA-BRUCEI, Molecular and biochemical parasitology, 91(1), 1998, pp. 153-164
The purpose of this review is to consider recent results obtained conc
erning 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 bac
terial PI-PLCs than previously realised is described. The variant spec
ific 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 whe
ther this hydrolysis of the GPI-anchor plays any role during the life
cycle a GPI-PLC null mutant has been made. The phenotype indicates tha
t the gene is non-essential, but its absence alters the course of infe
ction in mice. (C) 1998 Francqui Foundation. Published by Elsevier Sci
ence B.V. All rights reserved.