Evidence map›Paper›PMID 22937752›Full record

ArticleAntioxidants & redox signaling2013

A glutathione-dependent detoxification system is required for formaldehyde resistance and optimal survival of Neisseria meningitidis in biofilms.

Nathan H Chen, Rafael M Couñago, Karrera Y Djoko, Michael P Jennings, Michael A Apicella, Bostjan Kobe, Alastair G McEwan

Open access · greenAbstract read
In one paragraph

Article in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

  1. The glutathione pathway is required for biofilm formation inCurrent research in microbial sciences · 2026
    Article
  2. Review
  3. Article
  4. Article
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  7. Molecular dissection of a dedicated formaldehyde dehydrogenase from Mycobacterium smegmatis.Protein science : a publication of the Protein Society · 2022
    Article
  8. Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022
    Article
  9. Review
  10. Review
  11. Newly discoveredADMET & DMPK · 2022
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  14. Article
  15. 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

7 authors at 3 institutions in 2 countries.

Nathan H ChenAustralian Centre for Infectious Disease Research, School of Chemistry and Molecular Biosciences, Faculty of Science, The University of Queensland, St. Lucia, Australia.
Rafael M Couñago
Karrera Y Djoko
Michael P Jennings
Michael A Apicella
Bostjan Kobe
Alastair G McEwan
The University of Queensland · AUGriffith University · AUUniversity of Iowa · US

Funding

Pulmonary Toxicology Facility CoreP30ES005605 · NIEHS · UNIVERSITY OF IOWA · PI HANS-JOACHIM LEHMLER · 1990 to 2026
$40.5M
NIEHS NIH HHS P30 ES005605
6 · The paper itself

Abstract

aimThe glutathione-dependent AdhC-EstD formaldehyde detoxification system is found in eukaryotes and prokaryotes. It is established that it confers protection against formaldehyde that is produced from environmental sources or methanol metabolism. Thus, its presence in the human host-adapted bacterial pathogen Neisseria meningitidis is intriguing. This work defined the biological function of this system in the meningococcus using phenotypic analyses of mutants linked to biochemical and structural characterization of purified enzymes.

resultsWe demonstrated that mutants in the adhC and/or estD were sensitive to killing by formaldehyde. Inactivation of adhC and/or estD also led to a loss of viability in biofilm communities, even in the absence of exogenous formaldehyde. Detailed biochemical and structural analyses of the esterase component demonstrated that S-formylglutathione was the only biologically relevant substrate for EstD. We further showed that an absolutely conserved cysteine residue was covalently modified by S-glutathionylation. This leads to inactivation of EstD. INNOVATION: The results provide several conceptual innovations. They provide a new insight into formaldehyde detoxification in bacteria that do not generate formaldehyde during the catabolism of methanol. Our results also indicate that the conserved cysteine, found in all EstD enzymes from humans to microbes, is a site of enzyme regulation, probably via S-glutathionylation.

conclusionThe adhc-estD system protects against formaldehyde produced during endogenous metabolism.

Indexed as

Aldehyde OxidoreductasesBiofilmsDrug Resistance, BacterialFormaldehydeNeisseria meningitidisStructure-Activity RelationshipThiolester HydrolasesAldehyde OxidoreductasesFormaldehydeformaldehyde dehydrogenase (glutathione)Thiolester Hydrolases

Identifiers

PMID22937752
PMCPMC3555115
OpenAlexW1967167016

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.