Evidence map›Paper›PMID 32513978›Full record

ArticleScientific reports2020

Role of Superoxide Reductase FA796 in Oxidative Stress Resistance in Filifactor alocis.

Arunima Mishra, Ezinne Aja, Hansel M Fletcher

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Functional Characterization of a Putative Sortase FA1364 inInternational journal of molecular sciences · 2026
    Article
  2. Frontiers in cellular and infection microbiology · 2026
    Article
  3. Transcription regulator TrtA modulates oxygen stress response inApplied and environmental microbiology · 2025
    Article
  4. Article
  5. The impact ofFrontiers in dental medicine · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Frontiers in oral health · 2022
    Review
  11. Article
  12. Article
  13. Journal of dental research · 2021
    Article
  14. Article
  15. 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

3 authors at 1 institution in 1 country.

Arunima MishraDivision of Microbiology and Molecular Genetics, Department of Basic Sciences, School of Medicine, Loma Linda University, Loma Linda, California, USA. amishra@llu.edu.
Ezinne AjaDivision of Microbiology and Molecular Genetics, Department of Basic Sciences, School of Medicine, Loma Linda University, Loma Linda, California, USA.
Hansel M FletcherDivision of Microbiology and Molecular Genetics, Department of Basic Sciences, School of Medicine, Loma Linda University, Loma Linda, California, USA.
Loma Linda University · US

Funding

Mechanisms for adaptation to oxidative stress in Porphyromonas gingivalisR01DE019730 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2009 to 2013
$2.0M
Studies on the virulence regulation in PorphyromonasR01DE025852 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2016 to 2020
$2.0M
ECF sigma factors in adaptation and virulence of Porphyromonas gingivalisR01DE022508 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2012 to 2016
$1.8M
Studies on the virulence regulation in PorphyromonasR56DE013664 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2014 to 2014
$291k
NIDCR NIH HHS R01 DE019730NIDCR NIH HHS R01 DE022508NIDCR NIH HHS R01 DE025852NIDCR NIH HHS R56 DE013664
6 · The paper itself

Abstract

Filifactor alocis, a Gram-positive anaerobic bacterium, is now a proposed diagnostic indicator of periodontal disease. Because the stress response of this bacterium to the oxidative environment of the periodontal pocket may impact its pathogenicity, an understanding of its oxidative stress resistance strategy is vital. Interrogation of the F. alocis genome identified the HMPREF0389_00796 gene that encodes for a putative superoxide reductase (SOR) enzyme. SORs are non-heme, iron-containing enzymes that can catalyze the reduction of superoxide radicals to hydrogen peroxide and are important in the protection against oxidative stress. In this study, we have functionally characterized the putative SOR (FA796) from F. alocis ATCC 35896. The recombinant FA796 protein, which is predicted to be a homotetramer of the 1Fe-SOR class, can reduce superoxide radicals. F. alocis FLL141 (∆FA796::ermF) was significantly more sensitive to oxygen/air exposure compared to the parent strain. Sensitivity correlated with the level of intracellular superoxide radicals. Additionally, the FA796-defective mutant had increased sensitivity to hydrogen peroxide-induced stress, was inhibited in its ability to form biofilm and had reduced survival in epithelial cells. Collectively, these results suggest that the F. alocis SOR protein is a key enzymatic scavenger of superoxide radicals and protects the bacterium from oxidative stress conditions.

Indexed as

Amino Acid SequenceBiofilmsCells, CulturedEpithelial CellsEubacterialesHumansHydrogen PeroxideOxidation-ReductionOxidative StressOxidoreductasesRecombinant ProteinsHydrogen PeroxideOxidoreductasesRecombinant Proteinssuperoxide reductase

Identifiers

PMID32513978
PMCPMC7280497
OpenAlexW3033905006

What OpenQuestion holds

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LicenceCC BY
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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.