Evidence map›Paper›PMID 30742695›Full record

ArticlePLoS pathogens2019

The tyrosine transporter of Toxoplasma gondii is a member of the newly defined apicomplexan amino acid transporter (ApiAT) family.

Kathryn E R Parker, Stephen J Fairweather, Esther Rajendran, Martin Blume, Malcolm J McConville, Stefan Bröer, Kiaran Kirk, Giel G van Dooren

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. PfApiAT2 is a proline transporter essential for the transmission ofbioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Orthologs ofMicrobiology spectrum · 2024
    Article
  12. A pyruvate transporter in the apicoplast of apicomplexan parasites.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Kathryn E R ParkerResearch School of Biology, Australian National University, Canberra, ACT, Australia.ORCID 0000-0001-9245-8139
Stephen J FairweatherResearch School of Biology, Australian National University, Canberra, ACT, Australia.ORCID 0000-0003-1530-7876
Esther RajendranResearch School of Biology, Australian National University, Canberra, ACT, Australia.
Martin BlumeDepartment of Biochemistry and Molecular Biology and the Bio21 Institute of Molecular Science and Biotechnology, University of Melbourne, Parkville, VIC, Australia.ORCID 0000-0002-6894-3000
Malcolm J McConvilleDepartment of Biochemistry and Molecular Biology and the Bio21 Institute of Molecular Science and Biotechnology, University of Melbourne, Parkville, VIC, Australia.ORCID 0000-0002-7107-7887
Stefan BröerResearch School of Biology, Australian National University, Canberra, ACT, Australia.ORCID 0000-0002-8040-1634
Kiaran KirkResearch School of Biology, Australian National University, Canberra, ACT, Australia.ORCID 0000-0002-5613-2622
Giel G van DoorenResearch School of Biology, Australian National University, Canberra, ACT, Australia.ORCID 0000-0003-2455-9821
Australian National University · AUThe University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apicomplexan parasites are auxotrophic for a range of amino acids which must be salvaged from their host cells, either through direct uptake or degradation of host proteins. Here, we describe a family of plasma membrane-localized amino acid transporters, termed the Apicomplexan Amino acid Transporters (ApiATs), that are ubiquitous in apicomplexan parasites. Functional characterization of the ApiATs of Toxoplasma gondii indicate that several of these transporters are important for intracellular growth of the tachyzoite stage of the parasite, which is responsible for acute infections. We demonstrate that the ApiAT protein TgApiAT5-3 is an exchanger for aromatic and large neutral amino acids, with particular importance for L-tyrosine scavenging and amino acid homeostasis, and that TgApiAT5-3 is critical for parasite virulence. Our data indicate that T. gondii expresses additional proteins involved in the uptake of aromatic amino acids, and we present a model for the uptake and homeostasis of these amino acids. Our findings identify a family of amino acid transporters in apicomplexans, and highlight the importance of amino acid scavenging for the biology of this important phylum of intracellular parasites.

Indexed as

Amino Acid Transport SystemsAnimalsApicomplexaBiological TransportHost-Parasite InteractionsIon TransportParasitesProtozoan ProteinsToxoplasmaTyrosineAmino Acid Transport SystemsProtozoan ProteinsTyrosine

Identifiers

PMID30742695
PMCPMC6386423
OpenAlexW2911515058

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.