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Adsorption of Components of the Plasma Kinin-forming System on the Surface of Porphyromonas gingivalis Involves Gingipains as the Major Docking Platforms.

Rapala-Kozik, Maria; Bras, Grazyna; Chruscicka, Barbara; Karkowska-Kuleta, Justyna; Sroka, Aneta; Herwald, Heiko LU ; Nguyen, Ky-Anh; Eick, Sigrun; Potempa, Jan and Kozik, Andrzej (2011) In Infection and Immunity Dec. p.797-805
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 P. gingivalis. The adsorption characteristics of mutant strains deficient in selected proteins of the cell envelope suggested that the surface-associated cysteine proteinases, gingipains,... (More)
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 P. 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 interactions in periodontal infections. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Infection and Immunity
volume
Dec
pages
797 - 805
publisher
American Society for Microbiology
external identifiers
  • wos:000286462000025
  • pmid:21098107
  • scopus:79251531089
ISSN
1098-5522
DOI
10.1128/IAI.00966-10
language
English
LU publication?
yes
id
588c100f-81eb-46e3-8f22-4ee4d24e4c7d (old id 1731650)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/21098107?dopt=Abstract
date added to LUP
2010-12-01 13:42:47
date last changed
2017-10-22 04:56:27
@article{588c100f-81eb-46e3-8f22-4ee4d24e4c7d,
  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 P. 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 interactions in periodontal infections.},
  author       = {Rapala-Kozik, Maria and Bras, Grazyna and Chruscicka, Barbara and Karkowska-Kuleta, Justyna and Sroka, Aneta and Herwald, Heiko and Nguyen, Ky-Anh and Eick, Sigrun and Potempa, Jan and Kozik, Andrzej},
  issn         = {1098-5522},
  language     = {eng},
  pages        = {797--805},
  publisher    = {American Society for Microbiology},
  series       = {Infection and Immunity},
  title        = {Adsorption of Components of the Plasma Kinin-forming System on the Surface of Porphyromonas gingivalis Involves Gingipains as the Major Docking Platforms.},
  url          = {http://dx.doi.org/10.1128/IAI.00966-10},
  volume       = {Dec},
  year         = {2011},
}