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PAI-2/SerpinB2 Inhibits Proteolytic Activity in a P. gingivalis-dominated Multispecies Bacterial Consortium
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- Neilands, Jessica (författare)
- Malmö högskola,Odontologiska fakulteten (OD)
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- Bikker, Floris (författare)
- Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam, Free University and University of Amsterdam, Amsterdam, The Netherlands
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- Kinnby, Bertil (författare)
- Malmö högskola,Odontologiska fakulteten (OD)
- (creator_code:org_t)
- Elsevier, 2016
- 2016
- Engelska.
- Ingår i: Archives of Oral Biology. - : Elsevier. - 0003-9969 .- 1879-1506. ; 70, s. 1-8
- Tidskriftsartikel (refereegranskat)
Abstract
Ämnesord
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- 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.
Nyckelord
- Host-pathogen interaction
- Mucosal immunology
- Protease inhibitor
- Plasminogen activator inhibitor type 2
- PAI-2
- SerpinB2
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