Evidence map›Paper›PMID 21098107›Full record

ArticleInfection and immunity2011

Adsorption of components of the plasma kinin-forming system on the surface of Porphyromonas gingivalis involves gingipains as the major docking platforms.

Maria Rapala-Kozik, Grazyna Bras, Barbara Chruscicka, Justyna Karkowska-Kuleta, Aneta Sroka, Heiko Herwald, Ky-Anh Nguyen, Sigrun Eick, Jan Potempa, Andrzej Kozik

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2011. 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
1.8field-weighted citation impact, top 16% 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, 48 citations in OpenAlex.

  1. Article
  2. Review
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  6. Review
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  14. Review
  15. Virulence Associated Gene 8 ofFrontiers in immunology · 2018
    Article
  16. Manipulation of Neutrophils byFrontiers in cellular and infection microbiology · 2017
    Review
  17. Article
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  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

10 authors at 5 institutions in 5 countries.

Maria Rapala-KozikDepartment of Analytical Biochemistry, Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland.
Grazyna Bras
Barbara Chruscicka
Justyna Karkowska-Kuleta
Aneta Sroka
Heiko Herwald
Ky-Anh Nguyen
Sigrun Eick
Jan Potempa
Andrzej Kozik
Jagiellonian University · PLLund University · SESydney Dental Hospital · AUUniversity of Bern · CHUniversity of Louisville · US

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

Enhanced production of proinflammatory bradykinin-related peptides, the kinins, has been suggested to contribute to the pathogenesis of periodontitis, a common inflammatory disease of human gingival tissues. In this report, we describe a plausible mechanism of activation of the kinin-generating system, also known as the contact system or kininogen-kallikrein-kinin system, by the adsorption of its plasma-derived components such as high-molecular-mass kininogen (HK), prekallikrein (PK), and Hageman factor (FXII) to the cell surface of periodontal pathogen Porphyromonas gingivalis. The adsorption characteristics of mutant strains deficient in selected proteins of the cell envelope suggested that the surface-associated cysteine proteinases, gingipains, bearing hemagglutinin/adhesin domains (RgpA and Kgp) serve as the major platforms for HK and FXII adhesion. These interactions were confirmed by direct binding tests using microplate-immobilized gingipains and biotinylated contact factors. Other bacterial cell surface components such as fimbriae and lipopolysaccharide were also found to contribute to the binding of contact factors, particularly PK. Analysis of kinin release in plasma upon contact with P. gingivalis showed that the bacterial surface-dependent mechanism is complementary to the previously described kinin generation system dependent on HK and PK proteolytic activation by the gingipains. We also found that several P. gingivalis clinical isolates differed in the relative significance of these two mechanisms of kinin production. Taken together, these data show the importance of this specific type of bacterial surface-host homeostatic system interaction in periodontal infections.

Indexed as

Adhesins, BacterialAdsorptionBiotinylationCell MembraneCysteine EndopeptidasesGene Expression Regulation, BacterialGingipain Cysteine EndopeptidasesKininogensKininsMembrane ProteinsPorphyromonas gingivalisAdhesins, BacterialCysteine EndopeptidasesGingipain Cysteine EndopeptidasesKininogensKininsMembrane Proteins

Identifiers

PMID21098107
PMCPMC3028839
OpenAlexW1989930596

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.