Evidence map›Paper›PMID 27767067›Full record

ArticleScientific reports2016

The cytochrome bd-I respiratory oxidase augments survival of multidrug-resistant Escherichia coli during infection.

Mark Shepherd, Maud E S Achard, Adi Idris, Makrina Totsika, Minh-Duy Phan, Kate M Peters, Sohinee Sarkar, Cláudia A Ribeiro, Louise V Holyoake, Dimitrios Ladakis and 5 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

34 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. DistinctbioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Membrane-Bound Redox Enzyme CytochromeInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. Article
  12. Bioenergetics and Reactive Nitrogen Species in Bacteria.International journal of molecular sciences · 2022
    Review
  13. Recent Advances in Structural Studies of CytochromeInternational journal of molecular sciences · 2022
    Review
  14. Article
  15. Mechanistic and structural diversity between cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics.International journal of molecular sciences · 2021
    Review
  17. Review
  18. Article
  19. Bacterial Oxidases of the CytochromeAntioxidants & redox signaling · 2021
    Review
  20. ROS Defense Systems and Terminal Oxidases in Bacteria.Antioxidants (Basel, Switzerland) · 2021
    Review
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

15 authors at 4 institutions in 2 countries.

Mark ShepherdSchool of Biosciences, University of Kent, Canterbury, CT2 7NJ, United Kingdom.
Maud E S AchardSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Adi IdrisSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Makrina TotsikaSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Minh-Duy PhanSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Kate M PetersSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Sohinee SarkarSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Cláudia A RibeiroSchool of Biosciences, University of Kent, Canterbury, CT2 7NJ, United Kingdom.
Louise V HolyoakeSchool of Biosciences, University of Kent, Canterbury, CT2 7NJ, United Kingdom.
Dimitrios LadakisSchool of Biosciences, University of Kent, Canterbury, CT2 7NJ, United Kingdom.
Glen C UlettSchool of Medical Science, and Menzies Health Institute Queensland, Griffith University, Gold Coast, Queensland, 4222, Australia.
Matthew J SweetInstitute for Molecular Bioscience (IMB) and IMB Centre for Inflammation and Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.
Robert K PooleDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, United Kingdom.
Alastair G McEwanSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Mark A SchembriSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
University of Queensland · AUUniversity of Kent · GBGriffith University · AUUniversity of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E015883/1Biotechnology and Biological Sciences Research Council P18939
6 · The paper itself

Abstract

Nitric oxide (NO) is a toxic free radical produced by neutrophils and macrophages in response to infection. Uropathogenic Escherichia coli (UPEC) induces a variety of defence mechanisms in response to NO, including direct NO detoxification (Hmp, NorVW, NrfA), iron-sulphur cluster repair (YtfE), and the expression of the NO-tolerant cytochrome bd-I respiratory oxidase (CydAB). The current study quantifies the relative contribution of these systems to UPEC growth and survival during infection. Loss of the flavohemoglobin Hmp and cytochrome bd-I elicit the greatest sensitivity to NO-mediated growth inhibition, whereas all but the periplasmic nitrite reductase NrfA provide protection against neutrophil killing and promote survival within activated macrophages. Intriguingly, the cytochrome bd-I respiratory oxidase was the only system that augmented UPEC survival in a mouse model after 2 days, suggesting that maintaining aerobic respiration under conditions of nitrosative stress is a key factor for host colonisation. These findings suggest that while UPEC have acquired a host of specialized mechanisms to evade nitrosative stresses, the cytochrome bd-I respiratory oxidase is the main contributor to NO tolerance and host colonisation under microaerobic conditions. This respiratory complex is therefore of major importance for the accumulation of high bacterial loads during infection of the urinary tract.

Indexed as

Gene Expression Regulation, BacterialHost-Pathogen InteractionsAnimalsCytochrome b GroupCytochrome c GroupCytochromesDihydropteridine ReductaseDisease Models, AnimalDrug Resistance, Multiple, BacterialElectron Transport Chain Complex ProteinsEscherichia coli InfectionsEscherichia coli ProteinsHemeproteinsHumansMiceMice, Inbred C57BLcytochrome bd terminal oxidase complex, E coliCytochrome b Groupcytochrome C-552Cytochrome c GroupCytochromesDihydropteridine ReductaseElectron Transport Chain Complex ProteinsEscherichia coli ProteinsHemeproteinshmp protein, E coliNADH, NADPH OxidoreductasesNitric OxideOxidoreductasesYtfE protein, E coli

Identifiers

PMID27767067
PMCPMC5073308
OpenAlexW2535812261

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.