Abstract
THE mammalian malaria host–parasite systems seem particularly useful for studies aimed at elucidating the biochemical mechanisms of such interactions. During the vertebrate phase of their life cycles the malaria organisms are intracellular parasites of the red cell. The mature mammalian host red cell is also relatively simple metabolically; its energy metabolism is solely that of Embden–Meyerhof glycolysis and it also lacks the capacity for protein synthesis. We therefore studied several aspects of red cell glycolysis in monkeys heavily infected with Plasmodium knowlesi and mice heavily infected with P. berghei. In both these systems we have found an increase in red blood cell adenosine triphosphate (ATP) and a decrease in red cell 2,3-diphosphoglycerate (DPG). We also have evidence that these malaria parasites introduce a pyruvate kinase isozyme into their host red cells in amounts sufficient to alter red cell glycolysis. First, glycolytic intermediate data demonstrate an in vivo increase in pyruvate kinase activity in infected red cells; second, there is an increase in pyruvate kinase Vmax activity in infected cells; and third, gel electrophoretic patterns show a new pyruvate kinase isozyme in infected cells. We suggest that this alteration in red cell glycolysis is in a direction favourable to the parasite because it will increase red cell ATP at the expense of red cell DPG.
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OELSHLEGEL, F., SANDER, B. & BREWER, G. Pyruvate kinase in malaria host–parasite interaction. Nature 255, 345–347 (1975). https://doi.org/10.1038/255345a0
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DOI: https://doi.org/10.1038/255345a0
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