Evidence map›Paper›PMID 24366737›Full record

ArticleAntimicrobial agents and chemotherapy2014

Pharmacological assessment defines Leishmania donovani casein kinase 1 as a drug target and reveals important functions in parasite viability and intracellular infection.

Najma Rachidi, Jean François Taly, Emilie Durieu, Olivier Leclercq, Nathalie Aulner, Eric Prina, Pascale Pescher, Cedric Notredame, Laurent Meijer, Gerald F Späth

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Promastigote-to-Amastigote Conversion inPathogens (Basel, Switzerland) · 2022
    Review
  14. Microorganisms · 2021
    Review
  15. Article
  16. Review
  17. Identification of the Host Substratome ofFrontiers in cell and developmental biology · 2021
    Article
  18. Review
  19. SystematicFrontiers in chemistry · 2021
    Article
  20. Towards discovery of new leishmanicidal scaffolds able to inhibitJournal of enzyme inhibition and medicinal chemistry · 2020
    Article
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 5 institutions in 2 countries.

Najma RachidiInstitut Pasteur and CNRS URA2581, Unité de Parasitologie Moléculaire et Signalisation, Paris, France.
Jean François Taly
Emilie Durieu
Olivier Leclercq
Nathalie Aulner
Eric Prina
Pascale Pescher
Cedric Notredame
Laurent Meijer
Gerald F Späth
Institut Pasteur · FRStation Biologique de Roscoff · FRCentre National de la Recherche Scientifique · FRCentre for Genomic Regulation · ESPompeu Fabra University · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase inhibitors have emerged as new drugs in various therapeutic areas, including leishmaniasis, an important parasitic disease. Members of the Leishmania casein kinase 1 (CK1) family represent promising therapeutic targets. Leishmania casein kinase 1 isoform 2 (CK1.2) has been identified as an exokinase capable of phosphorylating host proteins, thus exerting a potential immune-suppressive action on infected host cells. Moreover, its inhibition reduces promastigote growth. Despite these important properties, its requirement for intracellular infection and its chemical validation as a therapeutic target in the disease-relevant amastigote stage remain to be established. In this study, we used a multidisciplinary approach combining bioinformatics, biochemical, and pharmacological analyses with a macrophage infection assay to characterize and define Leishmania CK1.2 as a valid drug target. We show that recombinant and transgenic Leishmania CK1.2 (i) can phosphorylate CK1-specific substrates, (ii) is sensitive to temperature, and (iii) is susceptible to CK1-specific inhibitors. CK1.2 is constitutively expressed at both the promastigote insect stage and the vertebrate amastigote stage. We further demonstrated that reduction of CK1 activity by specific inhibitors, such as D4476, blocks promastigote growth, strongly compromises axenic amastigote viability, and decreases the number of intracellular Leishmania donovani and L. amazonensis amastigotes in infected macrophages. These results underline the potential role of CK1 kinases in intracellular survival. The identification of differences in structure and inhibition profiles compared to those of mammalian CK1 kinases opens new opportunities for Leishmania CK1.2 antileishmanial drug development. Our report provides the first chemical validation of Leishmania CK1 protein kinases, required for amastigote intracellular survival, as therapeutic targets.

Indexed as

AnimalsBenzamidesCasein Kinase IConserved SequenceCricetinaeFemaleImidazolesIndolesIsoquinolinesLeishmania donovaniLeishmaniasis, VisceralMacrophagesMice, Inbred C57BLPhloroglucinolSequence AlignmentTrypanocidal Agents4-(4-(2,3-dihydrobenzo(1,4)dioxin-6-yl)-5-pyridin-2-yl-1H-imidazol-2-yl)benzamideBenzamidesCasein Kinase IIC 261ImidazolesIndolesIsoquinolinesN-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamidePhloroglucinolTrypanocidal Agents

Identifiers

PMID24366737
PMCPMC3957854
OpenAlexW2132551264

What OpenQuestion holds

Textmetadata
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.