Evidence map›Paper›PMID 17449654›Full record

ArticleEukaryotic cell2007

Carbohydrate metabolism in the Toxoplasma gondii apicoplast: localization of three glycolytic isoenzymes, the single pyruvate dehydrogenase complex, and a plastid phosphate translocator.

Tobias Fleige, Karsten Fischer, David J P Ferguson, Uwe Gross, Wolfgang Bohne

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
9.1field-weighted citation impact, top 1% of its field
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

73 citing papers in PubMed, 142 citations in OpenAlex.

  1. Article
  2. Review
  3. The apicoplast localized isocitrate dehydrogenase is needed forFrontiers in cellular and infection microbiology · 2025
    Article
  4. Article
  5. A pyruvate transporter in the apicoplast of apicomplexan parasites.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. TheeLife · 2024
    Article
  7. Review
  8. Comparative chemical genomics inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Identification of novel biomarkers for anti-Frontiers in microbiology · 2024
    Article
  10. TgKDAC4: A Unique Deacetylase ofMicroorganisms · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Parasite powerhouse: A review of the Toxoplasma gondii mitochondrion.The Journal of eukaryotic microbiology · 2022
    Review
  15. Article
  16. Review
  17. Mining the Proteome ofAnimals : an open access journal from MDPI · 2022
    Review
  18. Article
  19. Released Parasite-Derived Kinases as Novel Targets for Antiparasitic Therapies.Frontiers in cellular and infection microbiology · 2022
    Review
  20. Review

13 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 3 countries.

Tobias FleigeInstitute of Medical Microbiology, University of Göttingen, Kreuzbergring 57, D-37075 Göttingen, Germany.
Karsten Fischer
David J P Ferguson
Uwe Gross
Wolfgang Bohne
University of Göttingen · DEUiT The Arctic University of Norway · NOUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many apicomplexan parasites, such as Toxoplasma gondii and Plasmodium species, possess a nonphotosynthetic plastid, referred to as the apicoplast, which is essential for the parasites' viability and displays characteristics similar to those of nongreen plastids in plants. In this study, we localized several key enzymes of the carbohydrate metabolism of T. gondii to either the apicoplast or the cytosol by engineering parasites which express epitope-tagged fusion proteins. The cytosol contains a complete set of enzymes for glycolysis, which should enable the parasite to metabolize imported glucose into pyruvate. All the glycolytic enzymes, from phosphofructokinase up to pyruvate kinase, are present in the T. gondii genome, as duplicates and isoforms of triose phosphate isomerase, phosphoglycerate kinase, and pyruvate kinase were found to localize to the apicoplast. The mRNA expression levels of all genes with glycolytic products were compared between tachyzoites and bradyzoites; however, a strict bradyzoite-specific expression pattern was observed only for enolase I. The T. gondii genome encodes a single pyruvate dehydrogenase complex, which was located in the apicoplast and absent in the mitochondrion, as shown by targeting of epitope-tagged fusion proteins and by immunolocalization of the native pyruvate dehydrogenase complex. The exchange of metabolites between the cytosol and the apicoplast is likely to be mediated by a phosphate translocator which was localized to the apicoplast. Based on these localization studies, a model is proposed that explains the supply of the apicoplast with ATP and the reduction power, as well as the exchange of metabolites between the cytosol and the apicoplast.

Indexed as

Carbohydrate MetabolismToxoplasmaAmino Acid SequenceAnimalsGlycolysisIsoenzymesMolecular Sequence DataOrganellesPhosphate Transport ProteinsPlant ProteinsPlastidsProtozoan ProteinsPyruvate Dehydrogenase ComplexRecombinant Fusion ProteinsRNA, MessengerSequence AlignmentIsoenzymesPhosphate Transport ProteinsPlant ProteinsProtozoan ProteinsPyruvate Dehydrogenase ComplexRecombinant Fusion ProteinsRNA, Messenger

Identifiers

PMID17449654
PMCPMC1951530
OpenAlexW2153072978

What OpenQuestion holds

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Registered trials

None linked

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.