Reconstituted ferredoxin-MEP pathway of Apicomplexa in Escherichiacoli as an in situ screening platform for inhibitors and essential enzyme mutations.

ABSTRACT: The apicoplast, an essential plastid-like organelle of apicomplexan parasites, including Plasmodium spp. and Toxoplasma gondii, harbors unique metabolic pathways absent in the host. Within the apicoplast, the ferredoxin redox system consists of plant-type ferredoxin-NADP⁺ reductase (ptFNR) and its redox partner, plant-type ferredoxin (ptFd). It donates electrons to the last two enzymes in the essential methylerythritol phosphate (MEP) pathway of isoprenoid biosynthesis. To establish an easy-to-handle platform for screening for enzyme inhibitors or functional mutations of the Plasmodium falciparum MEP pathway in situ, we established an Escherichia coli model where bacterial growth depended on the last enzyme IspH and its redox system ptFd and ptFNR. For this, we supplemented a fl

SUBMITTER: Akuh OA 

PROVIDER: S-EPMC12605070 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature