THE PROPERTIES AND FUNCTION OF THE GLYCOSYLPHOSPHATIDYLINOSITOL-PHOSPHOLIPASE-C IN TRYPANOSOMA-BRUCEI

Citation
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
Citations number
57
Categorie Soggetti
Parasitiology
ISSN journal
01666851
Volume
91
Issue
1
Year of publication
1998
Pages
153 - 164
Database
ISI
SICI code
0166-6851(1998)91:1<153:TPAFOT>2.0.ZU;2-O
Abstract
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.