Transport of lactate and pyruvate in the intraerythrocytic malaria parasite, Plasmodium falciparum

The mature, intraerythrocytic form of the human malaria parasite, Plasmodiu m falciparum, is reliant on glycolysis for its energetic requirements. It p roduces large quantities of lactic acid, which have to be removed from the parasite's cytosol to maintain the cell's integrity and metabolic viability . Here we show that the monocarboxylates lactate and pyruvate an both trans ported across the parasite's plasma membrane via a H+/monocarboxylate sympo rt process that is saturable and inhibited by the bioflavonoid phloretin. T he results provide direct evidence for the presence at the parasite surface of a H+-coupled monocarboxylate transporter with features in common with m embers of the MCT (monocarboxylate transporter) family of higher eukaryotes .