Chapter 11 : Molecular Approaches to Malaria: Glycolysis in Asexual-Stage Parasites

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In erythrocytes, has no obvious energy stores. Glucose storage forms such as amylopectin and mannitol identified in other apicomplexan parasites are not reported in . The mitochondrion maintains a transmembrane potential gradient that is essential for survival and is a target for the antimalarial atovaquone; however, it is not used for aerobic glycolysis in asexual-stage parasites. Large quantities of lactic acid produced in the vicinity of hypoxic host tissue may impair function of host cells. There are, therefore, two independent reasons for targeting glycolysis in the postgenome era: first, to kill parasites by identifying new inhibitors and eventually developing novel drugs, and second, to decrease use of glucose and output of lactic acid in those regions where there are many parasites that could compete with host tissues for glucose and add to the problem of disposal of lactate. Increased metabolic activity of -infected red blood cells is accompanied by the appearance of glycolytic enzymes with properties distinct from host red blood cell enzymes. The most obvious way for inhibitors to target the action of glycolytic enzymes is by blocking their catalytic sites, which allows substrate analogs to be used as probes. Glucose transport may be a promising target on theoretical grounds; Lactate dehydrogenase (LDH) has received the most attention so far in terms of rational drug development. Glycolysis in may contribute to disease pathogenesis by competing for glucose in host tissues, lending added impetus to discovering ways of inhibiting this key pathway.

Citation: Woodrow C, Krishna S. 2005. Molecular Approaches to Malaria: Glycolysis in Asexual-Stage Parasites, p 223-233. In Sherman I (ed), Molecular Approaches to Malaria. ASM Press, Washington, DC. doi: 10.1128/9781555817558.ch11

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Major Facilitator Superfamily
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Postulated scheme for glycolytic reactions in -infected erythrocytes. Distinct cytosolic and apicoplast enzymes for TPI and pyruvate kinase are shown (see Table 1 ). Abbreviations: triosephosphate isomerase,TPI.For Enzyme Commission numbers, see Table 1 .

Citation: Woodrow C, Krishna S. 2005. Molecular Approaches to Malaria: Glycolysis in Asexual-Stage Parasites, p 223-233. In Sherman I (ed), Molecular Approaches to Malaria. ASM Press, Washington, DC. doi: 10.1128/9781555817558.ch11
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Generic image for table

In silico analysis of glycolytic enzymes of

Citation: Woodrow C, Krishna S. 2005. Molecular Approaches to Malaria: Glycolysis in Asexual-Stage Parasites, p 223-233. In Sherman I (ed), Molecular Approaches to Malaria. ASM Press, Washington, DC. doi: 10.1128/9781555817558.ch11

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