Roles of 1-Cys peroxiredoxin in haem detoxification in the human malaria parasite Plasmodium falciparum

摘要: In the present study, we investigated whether Plasmodium falciparum 1-Cys peroxiredoxin (Prx) (Pf1-Cys-Prx), a cytosolic protein expressed at high levels during haem-digesting stage, can act as an antioxidant to cope with oxidative burden of haem (ferriprotoporphyrin IX; FP). Recombinant Pf1-Cys-Prx (rPf1-Cys-Prx) competed glutathione (GSH) for FP and inhibited degradation by GSH. When rPf1-Cys-Prx was added GSH-mediated degradation, amount iron released reduced 23% reaction without (P < 0.01). The bound FP–agarose pH 7.4, which is pH parasite cytosol. could completely protect glutamine synthetase from inactivation dithiothreitol–Fe3+-dependent mixed-function oxidation system, it also protected enolase coincubation FP/GSH. Incubation white ghosts human red blood cells formation membrane associations 75% incubation findings study suggest that protects against stresses binding FP, slowing rate consequent generation, protecting proteins iron-derived reactive oxygen species, interfering membrane-associated FP.