Evidence map›Paper›PMID 27641616›Full record

ArticleScientific reports2016

TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to the inhibition of P. falciparum growth in human blood.

I Marginedas-Freixa, C Hattab, G Bouyer, F Halle, A Chene, S D Lefevre, M Cambot, A Cueff, M Schmitt, B Gamain and 5 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. TSPO protein binding partners in bacteria, animals, and plants.Journal of bioenergetics and biomembranes · 2021
    Review
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  6. Review
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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

15 authors at 3 institutions in 1 country.

I Marginedas-FreixaUMR_S1134, Université Sorbonne Paris Cité, Université Paris Diderot, Inserm, INTS, Unité Biologie Intégrée du Globule Rouge, Laboratoire d'Excellence GR-Ex, Paris, France.
C HattabUMR_S1134, Université Sorbonne Paris Cité, Université Paris Diderot, Inserm, INTS, Unité Biologie Intégrée du Globule Rouge, Laboratoire d'Excellence GR-Ex, Paris, France.
G BouyerUMR 8227 Comparative Erythrocyte's Physiology, CNRS, Université Pierre et Marie Curie, Sorbonne Universités, Laboratoire d'Excellence GR-Ex, F-29680 Roscoff, France.
F HalleUMR7200, Faculty of Pharmacy, University of Strasbourg, CNRS, 67400 Illkirch Graffenstaden, France.
A CheneUMR_S1134, Université Sorbonne Paris Cité, Université Paris Diderot, Inserm, INTS, Unité Biologie Intégrée du Globule Rouge, Laboratoire d'Excellence GR-Ex, Paris, France.
S D LefevreUMR_S1134, Université Sorbonne Paris Cité, Université Paris Diderot, Inserm, INTS, Unité Biologie Intégrée du Globule Rouge, Laboratoire d'Excellence GR-Ex, Paris, France.
M CambotUMR_S1134, Université Sorbonne Paris Cité, Université Paris Diderot, Inserm, INTS, Unité Biologie Intégrée du Globule Rouge, Laboratoire d'Excellence GR-Ex, Paris, France.
A CueffUMR 8227 Comparative Erythrocyte's Physiology, CNRS, Université Pierre et Marie Curie, Sorbonne Universités, Laboratoire d'Excellence GR-Ex, F-29680 Roscoff, France.
M SchmittUMR7200, Faculty of Pharmacy, University of Strasbourg, CNRS, 67400 Illkirch Graffenstaden, France.
B GamainUMR_S1134, Université Sorbonne Paris Cité, Université Paris Diderot, Inserm, INTS, Unité Biologie Intégrée du Globule Rouge, Laboratoire d'Excellence GR-Ex, Paris, France.
J J LacapereUMR 7203 LBM, CNRS, Université Pierre et Marie Curie, Sorbonne Universités, École Normale Supérieure - PSL Research University, Département de Chimie. F-75005 Paris, France.
S EgeeUMR 8227 Comparative Erythrocyte's Physiology, CNRS, Université Pierre et Marie Curie, Sorbonne Universités, Laboratoire d'Excellence GR-Ex, F-29680 Roscoff, France.
F BihelUMR7200, Faculty of Pharmacy, University of Strasbourg, CNRS, 67400 Illkirch Graffenstaden, France.
C Le Van KimUMR_S1134, Université Sorbonne Paris Cité, Université Paris Diderot, Inserm, INTS, Unité Biologie Intégrée du Globule Rouge, Laboratoire d'Excellence GR-Ex, Paris, France.
M A OstuniUMR_S1134, Université Sorbonne Paris Cité, Université Paris Diderot, Inserm, INTS, Unité Biologie Intégrée du Globule Rouge, Laboratoire d'Excellence GR-Ex, Paris, France.
Inserm · FRCentre National de la Recherche Scientifique · FRInternational Space University · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

After invading red blood cells (RBCs), Plasmodium falciparum (Pf) can export its own proteins to the host membrane and activate endogenous channels that are present in the membrane of RBCs. This transport pathway involves the Voltage Dependent Anion Channel (VDAC). Moreover, ligands of the VDAC partner TranSlocator PrOtein (TSPO) were demonstrated to inhibit the growth of the parasite. We studied the expression of TSPO and VDAC isoforms in late erythroid precursors, examined the presence of these proteins in membranes of non-infected and infected human RBCs, and evaluated the efficiency of TSPO ligands in inhibiting plasmodium growth, transporting the haem analogue Zn-protoporphyrin-IX (ZnPPIX) and enhancing the accumulation of reactive oxygen species (ROS). TSPO and VDAC isoforms are differentially expressed on erythroid cells in late differentiation states. TSPO2 and VDAC are present in the membranes of mature RBCs in a unique protein complex that changes the affinity of TSPO ligands after Pf infection. TSPO ligands dose-dependently inhibited parasite growth, and this inhibition was correlated to ZnPPIX uptake and ROS accumulation in the infected RBCs. Our results demonstrate that TSPO ligands can induce Pf death by increasing the uptake of porphyrins through a TSPO2-VDAC complex, which leads to an accumulation of ROS.

Indexed as

Amino Acid SequenceAnimalsAntigens, CD34Biological TransportCell DifferentiationErythrocyte MembraneErythrocytesErythroid CellsGene Expression ProfilingGlutathioneHumansLigandsMass SpectrometryParasitesPlasmodium falciparumProtein IsoformsAntigens, CD34GlutathioneLigandsProtein IsoformsProtoporphyrinsReactive Oxygen SpeciesReceptors, GABARNA, MessengerTSPO protein, humanVoltage-Dependent Anion Channelszinc protoporphyrin

Identifiers

PMID27641616
PMCPMC5027585
OpenAlexW2521297029

What OpenQuestion holds

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LicenceCC BY
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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.