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Article Dans Une Revue Experimental Parasitology Année : 1992

Plasmodium falciparum and Plasmodium chabaudi: Characterization of glycosylphosphatidylinositol-degrading activities

Résumé

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.

Dates et versions

hal-03246318 , version 1 (02-06-2021)

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Citer

Catherine Braun-Breton, Thierry Blisnick, Patricia Barbot, Roland Bülow, Luiz Pereira da Silva, et al.. Plasmodium falciparum and Plasmodium chabaudi: Characterization of glycosylphosphatidylinositol-degrading activities. Experimental Parasitology, 1992, 74 (4), pp.452-462. ⟨10.1016/0014-4894(92)90207-q⟩. ⟨hal-03246318⟩

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