PAI-2/SerpinB2 Inhibits Proteolytic Activity in a P. gingivalis-dominated Multispecies Bacterial Consortium

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PAI-2/SerpinB2 Inhibits Proteolytic Activity in a P. gingivalis-dominated Multispecies Bacterial Consortium

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Publication Article, peer reviewed scientific
Title PAI-2/SerpinB2 Inhibits Proteolytic Activity in a P. gingivalis-dominated Multispecies Bacterial Consortium
Author Neilands, Jessica ; Bikker, Floris ; Kinnby, Bertil
Date 2016
English abstract
Objective The aim of this study was to investigate the ability of the serine protease inhibitor plasminogen activator inhibitor type 2 (PAI-2/Serpin B2) to inhibit proteases produced by a multispecies bacterial consortium in vitro. Background Gingival and periodontal inflammation is associated with an increased flow of protein-rich gingival fluid. This nutritional change in the microenvironment favors bacteria with a proteolytic phenotype, triggering inflammation and associated tissue breakdown. PAI-2 is produced by macrophages and keratinocytes and is present in very high concentrations in gingival crevicular fluid; the highest level in the body. Design A multispecies bacterial consortium comprising nine bacterial strains, resembling the conditions in a periodontal pocket, was grown planktonically and as a biofilm. After seven days PAI-2 was added to the consortium and the proteolytic activity was assayed with fluorogenic protease substrates; FITC-labeled casein to detect global protease activity, fluorescent H-Gly-Pro-AMC for serine protease activity and fluorescent BIKKAM-10 for Porphyromonas gingivalis-associated protease activity. Protease activity associated with biofilm cells was examined by confocal scanning laser microscopy. Results PAI-2 inhibited proteolytic activity of the bacterial consortium, as seen by decreased fluorescence of all substrates. PAI-2 specifically inhibited P. gingivalis proteolytic activity. Conclusion To our knowledge, this is the first time that PAI-2 has been shown to inhibit bacterial proteases. Given the high concentration of PAI-2 in the gingival region, our results indicate that PAI-2 might play a role for the integrity of the epithelial barrier.
DOI https://doi.org/10.1016/j.archoralbio.2016.05.016 (link to publisher's fulltext.)
Link http://www.sciencedirect.com/science/article/pii/S... (external link to publication)
Publisher Elsevier
Host/Issue Archives of oral biology;
Volume 70
ISSN 0003-9969
Pages 1-8
Language eng (iso)
Subject Host-pathogen interaction
Mucosal immunology
Protease inhibitor
Plasminogen activator inhibitor type 2
PAI-2
SerpinB2
Medicine
Research Subject Categories::NATURAL SCIENCES
Handle http://hdl.handle.net/2043/23310 Permalink to this page
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