Evidence map›Paper›PMID 22798391›Full record

ArticleEukaryotic cell2012

A detoxifying oxygen reductase in the anaerobic protozoan Entamoeba histolytica.

João B Vicente, Vy Tran, Liliana Pinto, Miguel Teixeira, Upinder Singh

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 51 citations in OpenAlex.

  1. An iron-sulfur cluster as a new metal center in a flavodiiron protein.Protein science : a publication of the Protein Society · 2025
    Article
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  4. Episomal and chromosomal DNA replication and recombination inFrontiers in molecular biosciences · 2023
    Review
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  12. Review
  13. The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Review
  14. Dioxygen and nitric oxide scavenging by Treponema denticola flavodiiron protein: a mechanistic paradigm for catalysis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
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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

5 authors at 2 institutions in 2 countries.

João B VicenteDepartment of Internal Medicine, Stanford University School of Medicine, Stanford, California, USA.
Vy Tran
Liliana Pinto
Miguel Teixeira
Upinder Singh
Universidade Nova de Lisboa · PTStanford University · US

Funding

Investigating Entamoeba histolytica Colonic PathogenesisR01AI053724 · NIAID · STANFORD UNIVERSITY · PI SINGH, UPINDER · 2003 to 2012
$3.8M
NIAID NIH HHS AI-053724NIAID NIH HHS R01 AI053724
6 · The paper itself

Abstract

We report the characterization of a bacterial-type oxygen reductase abundant in the cytoplasm of the anaerobic protozoan parasite Entamoeba histolytica. Upon host infection, E. histolytica is confronted with various oxygen tensions in the host intestine, as well as increased reactive oxygen and nitrogen species at the site of local tissue inflammation. Resistance to oxygen-derived stress thus plays an important role in the pathogenic potential of E. histolytica. The genome of E. histolytica has four genes that encode flavodiiron proteins, which are bacterial-type oxygen or nitric oxide reductases and were likely acquired by lateral gene transfer from prokaryotes. The EhFdp1 gene has higher expression in virulent than in nonvirulent Entamoeba strains and species, hinting that the response to oxidative stress may be one correlate of virulence potential. We demonstrate that EhFdp1 is abundantly expressed in the cytoplasm of E. histolytica and that the protein levels are markedly increased (up to ~5-fold) upon oxygen exposure. Additionally, we produced fully functional recombinant EhFdp1 and demonstrated that this enzyme is a specific and robust oxygen reductase but has poor nitric oxide reductase activity. This observation represents a new mechanism of oxygen resistance in the anaerobic protozoan pathogen E. histolytica.

Indexed as

Entamoeba histolyticaGene Expression Regulation, EnzymologicOxidoreductasesOxygenProtozoan ProteinsOxidoreductasesOxygenProtozoan Proteins

Identifiers

PMID22798391
PMCPMC3445978
OpenAlexW2121157591

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.