Evidence map›Paper›PMID 28205520›Full record

ArticleNature communications2017

Cationic amino acid transporters play key roles in the survival and transmission of apicomplexan parasites.

Esther Rajendran, Sanduni V Hapuarachchi, Catherine M Miller, Stephen J Fairweather, Yeping Cai, Nicholas C Smith, Ian A Cockburn, Stefan Bröer, Kiaran Kirk, Giel G van Dooren

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

43 citing papers in PubMed, 75 citations in OpenAlex.

  1. A two-membrane gateway for monocarboxylates couples host glycolysis tobioRxiv : the preprint server for biology · 2026
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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

10 authors at 3 institutions in 1 country.

Esther RajendranResearch School of Biology, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Sanduni V HapuarachchiResearch School of Biology, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Catherine M MillerCollege of Public Health, Medical and Veterinary Sciences, James Cook University, Smithfield, Queensland 4878, Australia.
Stephen J FairweatherResearch School of Biology, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Yeping CaiJohn Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Nicholas C SmithQueensland Tropical Health Alliance Research Laboratory, Australian Institute of Tropical Health and Medicine, James Cook University, Smithfield, Queensland 4878, Australia.
Ian A CockburnJohn Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Stefan BröerResearch School of Biology, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Kiaran KirkResearch School of Biology, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Giel G van DoorenResearch School of Biology, Australian National University, Canberra, Australian Capital Territory 2601, Australia.ORCID 0000-0003-2455-9821
Australian National University · AUAustralian Institute of Tropical Health and Medicine · AUJames Cook University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apicomplexans are obligate intracellular parasites that scavenge essential nutrients from their hosts via transporter proteins on their plasma membrane. The identities of the transporters that mediate amino acid uptake into apicomplexans are unknown. Here we demonstrate that members of an apicomplexan-specific protein family-the Novel Putative Transporters (NPTs)-play key roles in the uptake of cationic amino acids. We show that an NPT from Toxoplasma gondii (TgNPT1) is a selective arginine transporter that is essential for parasite survival and virulence. We also demonstrate that a homologue of TgNPT1 from the malaria parasite Plasmodium berghei (PbNPT1), shown previously to be essential for the sexual gametocyte stage of the parasite, is a cationic amino acid transporter. This reveals a role for cationic amino acid scavenging in gametocyte biology. Our study demonstrates a critical role for amino acid transporters in the survival, virulence and life cycle progression of these parasites.

Indexed as

Amino Acid Transport Systems, BasicAnimalsApicomplexaArginineBiological TransportCell MembraneFemaleGametogenesisLife Cycle StagesMaleMembrane Transport ProteinsMiceMice, Inbred BALB COocytesParasitesPlasmodium bergheiAmino Acid Transport Systems, BasicArginineMembrane Transport ProteinsProtozoan ProteinsSodium-Phosphate Cotransporter Proteins, Type III

Identifiers

PMID28205520
PMCPMC5316894
OpenAlexW2588625032

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.