Evidence map›Paper›PMID 18458068›Full record

ArticleInfection and immunity2008

Characterization of a Helicobacter hepaticus putA mutant strain in host colonization and oxidative stress.

Navasona Krishnan, Alan R Doster, Gerald E Duhamel, Donald F Becker

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Pangenome comparison ofbioRxiv : the preprint server for biology · 2023
    Article
  3. Article
  4. Article
  5. Review
  6. Structural Biology of Proline Catabolic Enzymes.Antioxidants & redox signaling · 2019
    Review
  7. Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Structure, function, and mechanism of proline utilization A (PutA).Archives of biochemistry and biophysics · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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 1 institution in 1 country.

Navasona KrishnanDepartment of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.
Alan R Doster
Gerald E Duhamel
Donald F Becker
University of Nebraska–Lincoln · US

Funding

THE REDOX-MEDIATED REGULATION OF IRON-RESPONSIVE GENE EXPRESSION IN LIVERP20RR017675 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI GRASS, GREGOR · 2002 to 2011
$20.4M
Spectroelectrochemistry of the Novel PutA FlavoproteinR01GM061068 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI BECKER, DONALD F · 2001 to 2015
$3.7M
NCRR NIH HHS 5P-20-RR017675-03NCRR NIH HHS P20 RR017675NCRR NIH HHS P20 RR-017675-02NIGMS NIH HHS GM061068NIGMS NIH HHS R01 GM061068
6 · The paper itself

Abstract

Helicobacter hepaticus is a gram-negative, spiral-shaped microaerophilic bacterium associated with chronic intestinal infection leading to hepatitis and colonic and hepatic carcinomas in susceptible strains of mice. In the closely related human pathogen Helicobacter pylori, L-proline is a preferred respiratory substrate and is found at significantly high levels in the gastric juice of infected patients. A previous study of the proline catabolic PutA flavoenzymes from H. pylori and H. hepaticus revealed that Helicobacter PutA generates reactive oxygen species during proline oxidation by transferring electrons from reduced flavin to molecular oxygen. We further explored the preference for proline as a respiratory substrate and the potential impact of proline metabolism on the redox environment in Helicobacter species during host infection by disrupting the putA gene in H. hepaticus. The resulting putA knockout mutant strain was characterized by oxidative stress analysis and mouse infection studies. The putA mutant strain of H. hepaticus exhibited increased proline levels and resistance to oxidative stress relative to that of the wild-type strain, consistent with proline's role as an antioxidant. The significant increase in stress resistance was attributed to higher proline content, as no upregulation of antioxidant genes was observed for the putA mutant strain. The wild-type and putA mutant H. hepaticus strains displayed similar levels of infection in mice, but in mice challenged with the putA mutant strain, significantly reduced inflammation was observed, suggesting a role for proline metabolism in H. hepaticus pathogenicity in vivo.

Indexed as

AnimalsBacterial ProteinsCecumFecesHelicobacter hepaticusHelicobacter InfectionsHumansLiverMaleMembrane ProteinsMiceMutationOxidative StressOxidoreductases Acting on CH-NH Group DonorsProlineProline OxidaseBacterial ProteinsMembrane ProteinsOxidoreductases Acting on CH-NH Group DonorsProlineProline OxidasePutA protein, Bacteria

Identifiers

PMID18458068
PMCPMC2446744
OpenAlexW2122839142

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.