Evidence map›Paper›PMID 8226688›Full record

ArticleJournal of bacteriology1993

Hemin uptake in Porphyromonas gingivalis: Omp26 is a hemin-binding surface protein.

T E Bramanti, S C Holt

Abstract read
In one paragraph

Article in Journal of bacteriology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Detection of heme-binding proteins in epidemic strains of Burkholderia cepacia.Clinical and diagnostic laboratory immunology · 2001
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis.Microbiology and molecular biology reviews : MMBR · 1998
    Review
  16. Article
  17. Article
  18. Utilization of hemin and hemoglobin by Vibrio vulnificus biotype 2.Applied and environmental microbiology · 1996
    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

2 authors at 1 institution in 1 country.

T E BramantiDepartment of Periodontics, University of Texas Health Science Center at San Antonio 78284-7894.
S C Holt
The University of Texas Health Science Center at San Antonio · US

Funding

NIDCR NIH HHS DE00152NIDCR NIH HHS DE07267
6 · The paper itself

Abstract

A 26-kDa outer membrane protein (Omp26) has been proposed to play a role in hemin acquisition by Porphyromonas gingivalis (T. E. Bramanti and S. C. Holt, J. Bacteriol. 174:5827-5839, 1992). We studied [55Fe]hemin uptake in P. gingivalis grown under conditions of hemin starvation (Omp26 expressed on the outer membrane surface) and hemin excess (Omp26 not expressed on surface). [55Fe]hemin uptake occurred rapidly in hemin-starved cells which incorporated up to 70% of total [55Fe]hemin within 3 min. P. gingivalis grown under hemin-starved conditions or treated with the iron chelator 2,2'-bipyridyl to induce an iron stress took up six times more [55Fe]hemin than hemin-excess-grown cells. Polyclonal monospecific anti-Omp26 antibody added to hemin-starved cells inhibited [55Fe]hemin uptake by more than 50%, whereas preimmune serum had no effect. [55Fe]hemin uptake in hemin-starved P. gingivalis was inhibited (36 to 67%) in the presence of equimolar amounts of unlabeled hemin, protoporphyrin IX, zinz protoporphyrin, and Congo red dye but was not inhibited in the presence of non-hemin-containing iron sources. Heat shock treatment (45 degrees C) of hemin-excess-grown P. gingivalis (which cases translocation of Omp26 to the surface) increased [55Fe]hemin uptake by threefold after 3 min in comparison with cells grown at 37 degrees C. However, no [55Fe] hemin uptake beyond 3 min was observed in either hemin-excess-grown or hemin-starved cells exposed to heat shock. In experiments using heterobifunctional cross-linker analysis, hemin and selected porphyrins were cross-linked to Omp26 in hemin-starved P. gingivalis, but no cross-linking was seen with hemin-excess-grown cells. However, cross-linking of hemin to Omp26 was observed after heat shock treatment of hemin-excess-grown cells. Finally, anti-Omp26 antibody inhibited cross-linked of hemin to Omp26. These findings indicate that hemin binding and transport into P.gingivalis cell mediated by Omp26.

Indexed as

Bacterial Outer Membrane ProteinsBiological TransportCell MembraneCongo RedElectrophoresis, Polyacrylamide GelHeminHemoglobinsIronIron RadioisotopesKineticsMembrane ProteinsMolecular WeightPorphyromonas gingivalisProtease InhibitorsProtoporphyrinsBacterial Outer Membrane ProteinsCongo RedHeminHemoglobinsIronIron RadioisotopesMembrane ProteinsProtease Inhibitorsprotoporphyrin IXProtoporphyrinszinc protoporphyrin

Identifiers

PMID8226688
PMCPMC206886
OpenAlexW1934248043

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.