Evidence map›Paper›PMID 27562167›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

NADPH oxidase-derived H2O2 subverts pathogen signaling by oxidative phosphotyrosine conversion to PB-DOPA.

Luis A Alvarez, Lidija Kovačič, Javier Rodríguez, Jan-Hendrik Gosemann, Malgorzata Kubica, Gratiela G Pircalabioru, Florian Friedmacher, Ada Cean, Alina Ghişe, Mihai B Sărăndan and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. 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
2.6field-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

28 citing papers in PubMed, 39 citations in OpenAlex.

  1. De novo DUOX2 expression in neutrophil subsets shapes the pathogenesis of intestinal disease.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Cyclic Isothiocyanate Goitrin ImpairsPlants (Basel, Switzerland) · 2024
    Article
  3. Connection between protein-tyrosine kinase inhibition and coping with oxidative stress inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Review
  5. Article
  6. Transcriptomic Analysis ofAntioxidants (Basel, Switzerland) · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Hydrogen Peroxide Affects Growth ofFrontiers in immunology · 2021
    Article
  12. Oxidants in Physiological Processes.Handbook of experimental pharmacology · 2021
    Review
  13. Review
  14. Article
  15. Epithelial Toll-like receptors and their role in gut homeostasis and disease.Nature reviews. Gastroenterology & hepatology · 2020
    Review
  16. Article
  17. Control and dysregulation of redox signalling in the gastrointestinal tract.Nature reviews. Gastroenterology & hepatology · 2019
    Review
  18. Article
  19. Review
  20. 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

16 authors at 6 institutions in 4 countries.

Luis A AlvarezNational Children's Research Center, Our Lady's Children's Hospital Crumlin, Dublin 12, Ireland;
Lidija KovačičConway Institute, School of Medicine, University College Dublin, Dublin 4, Ireland;
Javier RodríguezSystems Biology Ireland, University College Dublin, Dublin 4, Ireland;
Jan-Hendrik GosemannNational Children's Research Center, Our Lady's Children's Hospital Crumlin, Dublin 12, Ireland;
Malgorzata KubicaConway Institute, School of Medicine, University College Dublin, Dublin 4, Ireland;
Gratiela G PircalabioruConway Institute, School of Medicine, University College Dublin, Dublin 4, Ireland;
Florian FriedmacherNational Children's Research Center, Our Lady's Children's Hospital Crumlin, Dublin 12, Ireland;
Ada CeanFaculty of Veterinary Medicine, Banat University of Agricultural Sciences and Veterinary Medicine "King Michael I of Romania", 300645 Timisoara, Romania;
Alina GhişeFaculty of Veterinary Medicine, Banat University of Agricultural Sciences and Veterinary Medicine "King Michael I of Romania", 300645 Timisoara, Romania;
Mihai B SărăndanFaculty of Veterinary Medicine, Banat University of Agricultural Sciences and Veterinary Medicine "King Michael I of Romania", 300645 Timisoara, Romania;
Prem PuriNational Children's Research Center, Our Lady's Children's Hospital Crumlin, Dublin 12, Ireland;
Simon DaffSchool of Chemistry, University of Edinburgh, Edinburgh EH9 3F, United Kingdom;
Erika PlettnerDepartment of Chemistry, Simon Fraser University, Burnaby, BC V5A 1S6, Canada.
Alex von KriegsheimSystems Biology Ireland, University College Dublin, Dublin 4, Ireland;
Billy BourkeNational Children's Research Center, Our Lady's Children's Hospital Crumlin, Dublin 12, Ireland; Conway Institute, School of Medicine, University College Dublin, Dublin 4, Ireland; billy.bourke@ucd.ie ulla.knaus@ucd.ie.
Ulla G KnausNational Children's Research Center, Our Lady's Children's Hospital Crumlin, Dublin 12, Ireland; Conway Institute, School of Medicine, University College Dublin, Dublin 4, Ireland; billy.bourke@ucd.ie ulla.knaus@ucd.ie.
University College Dublin · IENational Children’s Research Centre · IEUnivesity of Life Science "King Mihai I" from Timisoara · ROChildren's Health Ireland at Crumlin · IESimon Fraser University · CAUniversity of Edinburgh · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Strengthening the host immune system to fully exploit its potential as antimicrobial defense is vital in countering antibiotic resistance. Chemical compounds released during bidirectional host-pathogen cross-talk, which follows a sensing-response paradigm, can serve as protective mediators. A potent, diffusible messenger is hydrogen peroxide (H2O2), but its consequences on extracellular pathogens are unknown. Here we show that H2O2, released by the host on pathogen contact, subverts the tyrosine signaling network of a number of bacteria accustomed to low-oxygen environments. This defense mechanism uses heme-containing bacterial enzymes with peroxidase-like activity to facilitate phosphotyrosine (p-Tyr) oxidation. An intrabacterial reaction converts p-Tyr to protein-bound dopa (PB-DOPA) via a tyrosinyl radical intermediate, thereby altering antioxidant defense and inactivating enzymes involved in polysaccharide biosynthesis and metabolism. Disruption of bacterial signaling by DOPA modification reveals an infection containment strategy that weakens bacterial fitness and could be a blueprint for antivirulence approaches.

Indexed as

Campylobacter jejuniCell LineDihydroxyphenylalanineDrug Resistance, BacterialHemeHost-Pathogen InteractionsHumansHydrogen PeroxideImmune SystemKlebsiella pneumoniaeListeria monocytogenesNADPH OxidasesOxidation-ReductionOxidative PhosphorylationOxygenPeroxidaseDihydroxyphenylalanineHemeHydrogen PeroxideNADPH OxidasesOxygenPeroxidasePhosphotyrosineReactive Oxygen SpeciesTyrosinebacterial tyrosine phosphorylationDOPAmucosal immunityNADPH oxidasereactive oxygen species (ROS)

Identifiers

PMID27562167
PMCPMC5027431
OpenAlexW2515781598

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.