A P5-ATPase, TgFLP12, diverging from plant chloroplast lipid transporters mediates apicoplast fatty export in Toxoplasma

Christophe-Sébastien Arnold, Anna-Maria Alazzi, Serena Shunmugam, Jan Janouškovec, Laurence Berry, Sarah Charital, Thierry Gautier, Samuel Duley, Delphine Jublot, Catherine Lemaire-Vieille, Marie-France Cesbron-Delauw, Pierre Cavailles, Jérôme Govin, Nicholas J. Katris, Yoshiki Yamaryo-Botté and Cyrille Y. Botté ()
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Christophe-Sébastien Arnold: Université Grenoble Alpes
Anna-Maria Alazzi: Université Grenoble Alpes
Serena Shunmugam: Université Grenoble Alpes
Jan Janouškovec: Institute of Microbiology of the Czech Academy of Sciences
Laurence Berry: Université Montpellier
Sarah Charital: Université Grenoble Alpes
Thierry Gautier: Université Grenoble Alpes
Samuel Duley: Université Grenoble Alpes
Delphine Jublot: Université Grenoble Alpes
Catherine Lemaire-Vieille: Université Grenoble Alpes
Marie-France Cesbron-Delauw: Université Grenoble Alpes
Pierre Cavailles: Université Grenoble Alpes
Jérôme Govin: Université Grenoble Alpes
Nicholas J. Katris: Université Grenoble Alpes
Yoshiki Yamaryo-Botté: Université Grenoble Alpes
Cyrille Y. Botté: Université Grenoble Alpes

Nature Communications, 2025, vol. 16, issue 1, 1-16

Abstract: Abstract Toxoplasma gondii, an apicomplexan parasite and agent of the human disease toxoplasmosis, possesses a non-photosynthetic relic plastid, named the apicoplast. Thought to be evolved from a red algal plastid, the apicoplast houses major metabolic pathways, such as heme, isoprenoid and lipid synthesis, crucial for parasite survival, and thus considered attractive drug targets. However, despite similarities with plant chloroplast lipid synthesis pathways, the apicoplast lacks canonical plant/chloroplast lipid transporters and so metabolite import/export is at present, poorly characterised. Here we identify TgFLP12, a newly identified P5-ATPase transporter localised to the Toxoplasma apicoplast. TgFLP12 is found in the SAR (Stramenopile-Alveolata-Rhizaria) supergroup (to which belong Apicomplexa parasites and chromerids) but absent in higher plants. Disruption of TgFLP12 causes major defects on apicoplast morphology. Lipidomic analyses and stable isotope labelling reveal a unique accumulation of C14:0 in the apicoplast, which is then lacking in most major lipid classes subsequently synthesized in the ER. Successful complementation of a yeast mutant deficient in fatty acid transport with TgFLP12 validates TgFLP12 as a fatty acid transporter. Overall, we identify a potentially important drug target: the apicoplast fatty acid exporter, specific to Apicomplexa which unexpectedly also highlights Toxoplasma’s utility as a model organism for investigating algal biology.

Date: 2025
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DOI: 10.1038/s41467-025-61155-9

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