Plasmodium falciparum and Plasmodium chabaudi: characterization of glycosylphosphatidylinositol-degrading activities.

Abstract

Merozoites of malaria parasites have a membrane-bound serine protease whose solubilization and subsequent activity depend on a parasite-derived glycosylphosphatidylinositol-phospholipase C (GPI-PLC). The GPI-degrading activities from both Plasmodium falciparum and Plasmodium chabaudi have been characterized and partially purified by phenylboronate chromatography. They are membrane-bound, developmentally regulated, calcium-independent enzymes and as such they resemble GPI-PLC of Trypanosoma brucei. Furthermore, a T. brucei GPI-PLC-specific monoclonal antibody (mAT3) immunoprecipitates the plasmodial GPI-degrading activity. Thin-layer chromatography is suggestive of two activities: a GPI-PLC and a phospholipase A.

• Authors: C Braun-Breton, T Blisnick, P Barbot, R Bülow, L Pereira da Silva, G Langsley
• Journal: Experimental parasitology (Exp Parasitol) Vol. 74 Issue 4 Pg. 452-62 (Jun 1992) ISSN: 0014-4894 [Print] United States
• PMID: 1317298 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Glycolipids
• Glycosylphosphatidylinositols
• Phosphatidylinositols
• Phospholipases A
• Phosphoric Diester Hydrolases
• Type C Phospholipases
• Phosphatidylinositol Diacylglycerol-Lyase
• Glycosylphosphatidylinositol Diacylglycerol-Lyase

Topics

• Animals
• Cross Reactions
• Glycolipids (metabolism)
• Glycosylphosphatidylinositol Diacylglycerol-Lyase
• Glycosylphosphatidylinositols
• Phosphatidylinositol Diacylglycerol-Lyase
• Phosphatidylinositols (metabolism)
• Phospholipases A (immunology, isolation & purification, metabolism)
• Phosphoric Diester Hydrolases (immunology, isolation & purification, metabolism)
• Plasmodium chabaudi (enzymology)
• Plasmodium falciparum (enzymology)
• Trypanosoma brucei brucei (enzymology)
• Type C Phospholipases (immunology, isolation & purification, metabolism)