Status of Plasmodium falciparum towards catalase

The role of endogenous and internalized catalase in the protection of Plasmodium against oxidant stress was studied. Catalase activities were measured in isolated Plasmodium falciparum at different stages of intererythrocytic development. Activities measured at late schizont stages were compared to...

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Published inBritish journal of haematology Vol. 103; no. 1; pp. 52 - 59
Main Authors CLAREBOUT, G, SLOMIANNY, C, DELCOURT, P, LEU, B, MASSET, A, CAMUS, D, DIVE, D
Format Journal Article
LanguageEnglish
Published Oxford, U.K. and Cambridge, USA Blackwell Science Ltd 01.10.1998
Blackwell
Blackwell Publishing Ltd
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Summary:The role of endogenous and internalized catalase in the protection of Plasmodium against oxidant stress was studied. Catalase activities were measured in isolated Plasmodium falciparum at different stages of intererythrocytic development. Activities measured at late schizont stages were compared to parasite markers (glutamate dehydrogenase, SOD) and to red blood cell markers (haemoglobin, Cu/Zn‐SOD). The fate of the host cell catalase in the parasite digestive system was studied by immunoelectron microscopy using monoclonal antibodies. The internalized catalase appeared to be dissociated in the digestive system of the parasite and inactivated. To examine the protective role of the endogenous and internalized catalase in the parasite protection against oxidant stress, parasites were cultivated at two oxygen concentrations (5% and 20%) in inhibited catalase red blood cells. These experiments suggested that the catalases present both in red blood cell and parasite are not essential when parasites are cultivated under 5% oxygen, but are necessary to protect the parasite under 20% oxygen. Catalase may not be the main protective enzyme involved in the protection of P. falciparum in standard in vitro culture conditions, but may become critical under the higher oxygen tensions conditions encountered in vivo.
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ISSN:0007-1048
1365-2141
DOI:10.1046/j.1365-2141.1998.00946.x