The collagenase activity of<i>Porphyromonas gingivalis</i>is due to Arg-gingipain

Houle, M.A; Grenier, Daniel; Plamondon, Pascale; Nakayama, Koji

doi:10.1016/s0378-1097(03)00178-2

Cited by 55 publications

(41 citation statements)

References 19 publications

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“…Collagen degradation by periodontopathogens may thus be involved in gingival tissue destruction. The collagenolytic activity of P. gingivalis has been attributed to various proteinases (21,27). In the present study, we showed that AC-PACs inhibited collagen degradation by P. gingivalis in a dose-dependent manner, suggesting that ACPACs may contribute to reducing the destructive process.…”

Section: Discussionsupporting

confidence: 62%

Anti- Porphyromonas gingivalis and Anti-Inflammatory Activities of A-Type Cranberry Proanthocyanidins

Howell

Grenier

2010

Antimicrob Agents Chemother

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A-type cranberry proanthocyanidins (AC-PACs) have recently been reported to be beneficial for human health, especially urinary tract health. The effect of these proanthocyanidins on periodontitis, a destructive disease of tooth-supporting tissues, needs to be investigated. The purpose of this study was to investigate the effects of AC-PACs on various virulence determinants of Porphyromonas gingivalis as well as on the inflammatory response of oral epithelial cells stimulated by this periodontopathogen. We examined the effects of AC-PACs on P. gingivalis growth and biofilm formation, adherence to human oral epithelial cells and proteincoated surfaces, collagenase activity, and invasiveness. We also tested the ability of AC-PACs to modulate the P. gingivalis-induced inflammatory response by human oral epithelial cells. Our results showed that while AC-PACs neutralized all the virulence properties of P. gingivalis in a dose-dependent fashion, they did not interfere with growth. They also inhibited the secretion of interleukin-8 (IL-8) and chemokine (C-C motif) ligand 5 (CCL5) but did not affect the secretion of IL-6 by epithelial cells stimulated with P. gingivalis. This anti-inflammatory effect was associated with reduced activation of the nuclear factor-B (NF-B) p65 pathway. AC-PACs may be potentially valuable bioactive molecules for the development of new strategies to treat and prevent P. gingivalis-associated periodontal diseases.

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Section: Discussionsupporting

confidence: 62%

Anti- Porphyromonas gingivalis and Anti-Inflammatory Activities of A-Type Cranberry Proanthocyanidins

Howell

Grenier

2010

Antimicrob Agents Chemother

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“…The diversity of these enzymes is mainly correlated with the phylogenetic relationship of the three bacteria as follows: Clostridium, such as Clostridium histolyticum [7] and Clostridium perfringens [8]; Vibrio, such as Vibrio alginolyticus [9] and Vibrio parahaemolyticus [10]; and Porphyromonas, such as Porphyromonas gingivalis [11] and Porphyromonas endodontalis [12]. These microbes are pathogens or conditional pathogenic bacteria which potentially produce toxin.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Novel Collagenase from Bacillus pumilus Col-J

et al. 2009

Appl Biochem Biotechnol

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The collagenase, produced extracellular by Bacillus pumilus Col-J, was purified by ammonium sulfate precipitation followed by two gel filtrations, involving Sephadex G-100 column and Sepharose Fast Flow column. Purified collagenase has a 31.53-fold increase in specific activity of 87.33 U/mg and 7.00% recovery. The collagenase has a relative molecular weight of 58.64 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimal temperature for the enzyme reaction was 45 degrees C. More than 50% of the original activity still remained after 5 min of incubation at 70 degrees C or 10 min at 60 degrees C. The maximal enzyme activity of collagenase was obtained at pH 7.5, and it was stable over a pH range of 6.5-8.0. The collagenase activity was strongly inhibited by Mn(2+), Pb(2+), ethylenediamine tetraacetic acid, ethylene glycol tetraacetic acid, and beta-mercaptoethanol. However, Ca(2+) and Mg(2+) greatly increased its activity. The collagenase from B. pumilus Col-J showed highly specific activity towards the native collagen from calf skin. The K(m) and V(max) of the enzyme for collagen were 0.79 mg/mL and 129.5 U, respectively.

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“…These enzymes degrade collagens, constituents of extracellular matrix (ECM) found in vertebrate tissues, and contribute significantly to host tissue damage [18]. For instance, Arg gingipains, that are virulence factors produced by a periodontal pathogen P. gingivalis, possess collagenolytic activity [19]. Collagenase has been suggested as a putative virulence factor in F. columnare based on its absence in F. johnsoniae, a nonvirulent member of Flavobacteria, as revealed by suppressive subtractive hybridization analysis [35].…”

Section: Discussionmentioning

confidence: 99%

High Nutrient Concentration Can Induce Virulence Factor Expression and Cause Higher Virulence in an Environmentally Transmitted Pathogen

et al. 2016

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Environmentally transmitted opportunistic pathogens shuttle between two substantially different environments: outside-host and within-host habitats. These environments differ from each other especially with respect to nutrient availability. Consequently, the pathogens are required to regulate their behavior in response to environmental cues in order to survive, but how nutrients control the virulence in opportunistic pathogens is still poorly understood. In this study we examined how nutrient level in the outside-host environment affects the gene expression of putative virulence factors of the opportunistic fish pathogen Flavobacterium columnare. The impact of environmental nutrient concentration on bacterial virulence was explored by cultivating the bacteria in various nutrient conditions, measuring the gene expression of putative virulence factors with RTqPCR, and finally, experimentally challenging rainbow trout (Oncorhynchus mykiss) fry with these bacteria. Our results show that increased environmental nutrient concentration can increase the expression of putative virulence genes, chondroitinase (cslA) and collagenase, in the outside-host environment and may lead to more rapid fish mortality. These findings address that the environmental nutrients may act as significant triggers of virulence gene expression and therefore contribute to the interaction between an environmentally transmitted opportunistic pathogen and its host.

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The collagenase activity ofPorphyromonas gingivalisis due to Arg-gingipain

Cited by 55 publications

References 19 publications

Anti- Porphyromonas gingivalis and Anti-Inflammatory Activities of A-Type Cranberry Proanthocyanidins

Anti- Porphyromonas gingivalis and Anti-Inflammatory Activities of A-Type Cranberry Proanthocyanidins

Purification and Characterization of a Novel Collagenase from Bacillus pumilus Col-J

High Nutrient Concentration Can Induce Virulence Factor Expression and Cause Higher Virulence in an Environmentally Transmitted Pathogen

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