Effect of Erythrocyte Pyridoxal Kinase Activity on the In Vitro Growth Rates of Plasmodium falciparum

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Pyridoxal kinase is an essential enzyme for intracellular protein synthesis. It phosphorylates vitamin B₆ to its active coenzyme, pyridoxal-5’-phosphate, which then plays a central role in transamination and other critical biochemical reactions. Since Afro-Americans have a high frequency of the low erythrocyte pyridoxal kinase activity, it has been postulated that this enzyme defect may afford protection against fatal malaria infections. The in vitro growth rates of P. falciparum parasites were measured in erythrocytes with high, low and intermediate PLK enzyme activity and no significant difference in parasite growth rates was observed. Erythrocytes with low PLK activity were capable of supporting normal in vitro growth and development of P. falciparum parasites. Even though, P. falciparum parasites lack PLK activity, their complete dependence on red cell enzyme activity has yet to be established.