Evidence map›Paper›PMID 26082764›Full record

ArticleFrontiers in microbiology2015

The FAD-dependent glycerol-3-phosphate dehydrogenase of Giardia duodenalis: an unconventional enzyme that interacts with the g14-3-3 and it is a target of the antitumoral compound NBDHEX.

Marco Lalle, Serena Camerini, Serena Cecchetti, Renata Finelli, Gabriella Sferra, Joachim Müller, Giorgio Ricci, Edoardo Pozio

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Parasitology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Lipid Accumulation inMicroorganisms · 2023
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. The Nitrobenzoxadiazole Derivative NBDHEX Behaves asPharmaceuticals (Basel, Switzerland) · 2022
    Article
  11. Re-Discovery ofBiomedicines · 2021
    Article
  12. Nitroreductase Activites inPathogens (Basel, Switzerland) · 2021
    Article
  13. The Differential Growth Inhibition ofFrontiers in microbiology · 2021
    Article
  14. Review
  15. Review
  16. 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

8 authors at 3 institutions in 2 countries.

Marco LalleDepartment of Infectious, Parasitic and Immunomediated Diseases, Istituto Superiore di Sanità Rome, Italy.
Serena CameriniDepartment of Cell Biology and Neurosciences, Istituto Superiore di Sanità Rome, Italy.
Serena CecchettiDepartment of Cell Biology and Neurosciences, Istituto Superiore di Sanità Rome, Italy.
Renata FinelliDepartment of Infectious, Parasitic and Immunomediated Diseases, Istituto Superiore di Sanità Rome, Italy.
Gabriella SferraDepartment of Infectious, Parasitic and Immunomediated Diseases, Istituto Superiore di Sanità Rome, Italy.
Joachim MüllerInstitute of Parasitology, Vetsuisse Faculty, University of Bern Bern, Switzerland.
Giorgio RicciDepartment of Sciences and Chemical Technologies, University of Rome "Tor Vergata" Rome, Italy.
Edoardo PozioDepartment of Infectious, Parasitic and Immunomediated Diseases, Istituto Superiore di Sanità Rome, Italy.
Istituto Superiore di Sanità · ITUniversity of Bern · CHUniversity of Rome Tor Vergata · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The flagellated protozoan Giardia duodenalis is a worldwide parasite causing giardiasis, an acute and chronic diarrheal disease. Metabolism in G. duodenalis has a limited complexity thus making metabolic enzymes ideal targets for drug development. However, only few metabolic pathways (i.e., carbohydrates) have been described so far. Recently, the parasite homolog of the mitochondrial-like glycerol-3-phosphate dehydrogenase (gG3PD) has been identified among the interactors of the g14-3-3 protein. G3PD is involved in glycolysis, electron transport, glycerophospholipids metabolism, and hyperosmotic stress response, and is emerging as promising target in tumor treatment. In this work, we demonstrate that gG3PD is a functional flavoenzyme able to convert glycerol-3-phosphate into dihydroxyacetone phosphate and that its activity and the intracellular glycerol level increase during encystation. Taking advantage of co-immunoprecipitation assays and deletion mutants, we provide evidence that gG3PD and g14-3-3 interact at the trophozoite stage, the intracellular localization of gG3PD is stage dependent and it partially co-localizes with mitosomes during cyst development. Finally, we demonstrate that the gG3PD activity is affected by the antitumoral compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol, that results more effective in vitro at killing G. duodenalis trophozoites than the reference drug metronidazole. Overall, our results highlight the involvement of gG3PD in processes crucial for the parasite survival thus proposing this enzyme as target for novel antigiardial interventions.

Indexed as

14-3-3 proteinencystationenergy metabolismFAD-dependent glycerol-3-phoshate dehydrogenaseGiardia duodenalismitosomeNBDHEXnitroreduction

Identifiers

PMID26082764
PMCPMC4450592
OpenAlexW1590526322

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.