Evidence map›Paper›PMID 23336115›Full record

ArticleMolecular oral microbiology2013

Evidence of mutualism between two periodontal pathogens: co-operative haem acquisition by the HmuY haemophore of Porphyromonas gingivalis and the cysteine protease interpain A (InpA) of Prevotella intermedia.

D P Byrne, J Potempa, T Olczak, J W Smalley

Open access · greenAbstract read
In one paragraph

Article in Molecular oral microbiology, 2013. 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
4.4field-weighted citation impact, top 5% 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, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025
    Review
  7. Review
  8. Frontiers in cellular and infection microbiology · 2024
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Unique Properties of Heme Binding of theMolecules (Basel, Switzerland) · 2022
    Article
  15. Journal of oral microbiology · 2022
    Review
  16. International journal of molecular sciences · 2021
    Article
  17. Review
  18. Review
  19. International journal of molecular sciences · 2020
    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 3 institutions in 3 countries.

D P ByrneDepartment of Clinical Infection, Microbiology and Immunology, Institute of Infection and Global Health, University of Liverpool, Liverpool, UK.
J Potempa
T Olczak
J W Smalley
University of Liverpool · GBJagiellonian University · PLUniversity of Wrocław · PL

Funding

BACTERIAL PROTEINASES IN PERIODONTAL DISEASER01DE009761 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 1991 to 2012
$3.8M
NIDCR NIH HHS DE 09761NIDCR NIH HHS R01 DE009761
6 · The paper itself

Abstract

Haem (iron protoporphyrin IX) is both an essential growth factor and a virulence regulator of the periodontal pathogens Porphyromonas gingivalis and Prevotella intermedia, which acquire it through the proteolytic degradation of haemoglobin and other haem-carrying plasma proteins. The haem-binding lipoprotein HmuY haemophore and the gingipain proteases of P. gingivalis form a unique synthrophic system responsible for capture of haem from haemoglobin and methaemalbumin. In this system, methaemoglobin is formed from oxyhaemoglobin by the activities of gingipain proteases and serves as a facile substrate from which HmuY can capture haem. This study examined the possibility of cooperation between HmuY and the cysteine protease interpain A (InpA) of Pr. intermedia in the haem acquisition process. Using UV-visible spectroscopy and polyacrylamide gel electrophoresis, HmuY was demonstrated to be resistant to proteolysis and so able to cooperate with InpA to extract haem from haemoglobin, which was proteolytically converted to methaemoglobin by the protease. Spectroscopic pH titrations showed that both the iron(II) and iron(III) protoporphyrin IX-HmuY complexes were stable over the pH range 4-10, demonstrating that the haemophore could function over a range of pH that may be encountered in the dental plaque biofilm. This is the first demonstration of a bacterial haemophore working in conjunction with a protease from another bacterial species to acquire haem from haemoglobin and may represent mutualism between P. gingivalis and Pr. intermedia co-inhabiting the periodontal pocket.

Indexed as

Microbial InteractionsAdhesins, BacterialCysteine EndopeptidasesCysteine ProteasesGingipain Cysteine EndopeptidasesHemeHemeproteinsHydrogen-Ion ConcentrationMethemoglobinMultiprotein ComplexesOxyhemoglobinsPorphyromonas gingivalisPrevotella intermediaProtoporphyrinsAdhesins, BacterialCysteine EndopeptidasesCysteine ProteasesGingipain Cysteine EndopeptidasesHemeHemeproteinsiron protoporphyrin IXMethemoglobinMultiprotein ComplexesOxyhemoglobinsProtoporphyrins

Identifiers

PMID23336115
PMCPMC4180662
OpenAlexW2058226623

What OpenQuestion holds

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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.