Evidence map›Paper›PMID 12591874›Full record

ArticleJournal of bacteriology2003

Exogenous glutathione completes the defense against oxidative stress in Haemophilus influenzae.

Bjorn Vergauwen, Frederik Pauwels, Mario Vaneechoutte, Jozef J Van Beeumen

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.9field-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

28 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Diverse roles of low-molecular weight thiol GSH inCurrent research in microbial sciences · 2024
    Article
  3. Article
  4. Article
  5. Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Haemophilus influenzae and oxidative stress.Frontiers in cellular and infection microbiology · 2012
    Review
  18. Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Bjorn VergauwenLaboratory for Protein Biochemistry and Protein Engineering, Ghent University, Belgium.
Frederik Pauwels
Mario Vaneechoutte
Jozef J Van Beeumen
Ghent University · BEGhent University Hospital · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since they are equipped with several strategies by which they evade the antimicrobial defense of host macrophages, it is surprising that members of the genus Haemophilus appear to be deficient in common antioxidant systems that are well established to protect prokaryotes against oxidative stress. Among others, no genetic evidence for glutathione (gamma-Glu-Cys-Gly) (GSH) biosynthesis or for alkyl hydroperoxide reduction (e.g., the Ahp system characteristic or enteric bacteria) is apparent from the Haemophilus influenzae Rd genome sequence, suggesting that the organism relies on alternative systems to maintain redox homeostasis or to reduce small alkyl hydroperoxides. In this report we address this apparent paradox for the nontypeable H. influenzae type strain NCTC 8143. Instead of biosynthesis, we could show that this strain acquires GSH by importing the thiol tripeptide from the growth medium. Although such GSH accumulation had no effect on growth rates, the presence of cellular GSH protected against methylglyoxal, tert-butyl hydroperoxide (t-BuOOH), and S-nitrosoglutathione toxicity and regulated the activity of certain antioxidant enzymes. H. influenzae NCTC 8143 extracts were shown to contain GSH-dependent peroxidase activity with t-BuOOH as the peroxide substrate. The GSH-mediated protection against t-BuOOH stress is most probably catalyzed by the product of open reading frame HI0572 (Prx/Grx), which we isolated from a genomic DNA fragment that confers wild-type resistance to t-BuOOH toxicity in the Ahp-negative Escherichia coli strain TA4315 and that introduces GSH-dependent alkyl hydroperoxide reductase activity into naturally GSH peroxidase-negative E. coli. Finally, we demonstrated that cysteine is an essential amino acid for growth and that cystine, GSH, glutathione amide, and cysteinylglycine can be catabolized in order to complement cysteine deficiency.

Indexed as

Oxidative StressAntioxidantsCatalaseCloning, MolecularDrug Resistance, MicrobialEscherichia coliGenetic Complementation TestGlutathioneGlutathione PeroxidaseHaemophilus influenzaeInactivation, MetabolicMutationPhagocytosisPyruvaldehydeS-NitrosoglutathioneSulfurAntioxidantsCatalaseGlutathioneglutathione amideGlutathione PeroxidasePyruvaldehydeS-NitrosoglutathioneSulfurtert-Butylhydroperoxide

Identifiers

PMID12591874
PMCPMC148052
OpenAlexW2107106263

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.