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- W4384665185 abstract "To ensure their survival in the human bloodstream, malaria parasites degrade up to 80% of the host erythrocyte hemoglobin in an acidified digestive vacuole. Here, we combine conditional reverse genetics and quantitative imaging approaches to demonstrate that the human malaria pathogen Plasmodium falciparum employs a heteromultimeric V-ATPase complex to acidify the digestive vacuole matrix, which is essential for intravacuolar hemoglobin release, heme detoxification, and parasite survival. We reveal an additional function of the membrane-embedded V-ATPase subunits in regulating morphogenesis of the digestive vacuole independent of proton translocation. We further show that intravacuolar accumulation of antimalarial chemotherapeutics is surprisingly resilient to severe deacidification of the vacuole and that modulation of V-ATPase activity does not affect parasite sensitivity toward these drugs." @default.
- W4384665185 created "2023-07-20" @default.
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- W4384665185 date "2023-07-18" @default.
- W4384665185 modified "2023-10-18" @default.
- W4384665185 title "The role of <i>Plasmodium</i> V-ATPase in vacuolar physiology and antimalarial drug uptake" @default.
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- W4384665185 doi "https://doi.org/10.1073/pnas.2306420120" @default.
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