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© François Rodhain
Plasmodium malariae (un des quatre hématozoaires qui parasitent l'homme), agent du paludisme, dans un frottis de sang humain. Stade trophozoïte. Coloration de May-Grünwald Giemsa.
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cell reports - 14 Jun 2022

Wagner MP, Formaglio P, Gorgette O, Dziekan JM, Huon C, Berneburg I, Rahlfs S, Barale JC, Feinstein SI, Fisher AB, Ménard D, Bozdech Z, Amino R, Touqui L, Chitnis CE,

Link to Pubmed [PMID] – 35705035

Link to DOI – 10.1016/j.celrep.2022.110923

Cell Rep 2022 Jun; 39(11): 110923

The uptake and digestion of host hemoglobin by malaria parasites during blood-stage growth leads to significant oxidative damage of membrane lipids. Repair of lipid peroxidation damage is crucial for parasite survival. Here, we demonstrate that Plasmodium falciparum imports a host antioxidant enzyme, peroxiredoxin 6 (PRDX6), during hemoglobin uptake from the red blood cell cytosol. PRDX6 is a lipid-peroxidation repair enzyme with phospholipase A2 (PLA2) activity. Inhibition of PRDX6 with a PLA2 inhibitor, Darapladib, increases lipid-peroxidation damage in the parasite and disrupts transport of hemoglobin-containing vesicles to the food vacuole, causing parasite death. Furthermore, inhibition of PRDX6 synergistically reduces the survival of artemisinin-resistant parasites following co-treatment of parasite cultures with artemisinin and Darapladib. Thus, PRDX6 is a host-derived drug target for development of antimalarial drugs that could help overcome artemisinin resistance.

https://pubmed.ncbi.nlm.nih.gov/35705035