Evidence map›Paper›PMID 40595705›Full record

ArticleNature communications2025

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 and 6 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors.

Christophe-Sébastien ArnoldApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.ORCID http://orcid.org/0000-0002-2392-5837
Anna-Maria AlazziTeam Govin, Institute for Advanced Biosciences, CNRS UMR5309, INSERM U1209, Université Grenoble Alpes, Grenoble, France.
Serena ShunmugamApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.ORCID http://orcid.org/0000-0001-6179-3292
Jan JanouškovecCentre Algatech, Institute of Microbiology of the Czech Academy of Sciences, Novohradská 237, Třeboň, Czech Republic.ORCID http://orcid.org/0000-0001-6547-749X
Laurence BerryLaboratory of Pathogen Host Interactions, Université Montpellier, Montpellier, France.
Sarah CharitalApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.
Thierry GautierTeam Govin, Institute for Advanced Biosciences, CNRS UMR5309, INSERM U1209, Université Grenoble Alpes, Grenoble, France.
Samuel DuleyApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.
Delphine JublotApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.
Catherine Lemaire-VieilleApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.
Marie-France Cesbron-DelauwApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.
Pierre CavaillesApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.ORCID http://orcid.org/0000-0001-5559-8634
Jérôme GovinTeam Govin, Institute for Advanced Biosciences, CNRS UMR5309, INSERM U1209, Université Grenoble Alpes, Grenoble, France.
Nicholas J KatrisApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.
Yoshiki Yamaryo-BottéApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.
Cyrille Y BottéApicolipid Team, Institute for Advanced Biosciences, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France. cyrille.botte@univ-grenoble-alpes.fr.ORCID http://orcid.org/0000-0002-2245-536X

Funding

Agence Nationale de la Recherche (French National Research Agency) ApicoLipidAdapt ANR-21-CE44-0010Agence Nationale de la Recherche (French National Research Agency) ApicolipidTraffic ANR-23-CE15-0009-01Agence Nationale de la Recherche (French National Research Agency) Labex Parafrap ANR-11-LABX-0024Agence Nationale de la Recherche (French National Research Agency) OIL ANR-24-CE15-2171-02Akademie Věd České Republiky (Academy of Sciences of the Czech Republic) Junior Start Grant 21-19798MCentre National de la Recherche Scientifique (National Center for Scientific Research) IRP ApicolipidFondation pour la Recherche Médicale (Foundation for Medical Research in France) FRM EQU202103012700Indo-French Centre for the Promotion of Advanced Research (Centre Franco-Indien pour la Promotion de la Recherche Avancée) 6003-1Institut National de la Santé et de la Recherche Médicale (National Institute of Health and Medical Research) IRP ApicolipidRégion Auvergne-Rhône-Alpes (Region Auvergne-Rhône-Alpes) IRICE Grant GEMELI
6 · The paper itself

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.

Indexed as

Adenosine TriphosphatasesApicoplastsChloroplastsFatty AcidsProtozoan ProteinsToxoplasmaBiological TransportLipid MetabolismPhylogenyPlastidsAdenosine TriphosphatasesFatty AcidsProtozoan Proteins

Identifiers

PMID40595705
PMCPMC12217143

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.