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PAI-2/SerpinB2 Inhibits Proteolytic Activity in a P. gingivalis-dominated Multispecies Bacterial Consortium
Malmö högskola, Faculty of Odontology (OD).
Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam, Free University and University of Amsterdam, Amsterdam, The Netherlands.
Malmö högskola, Faculty of Odontology (OD).
2016 (English)In: Archives of Oral Biology, ISSN 0003-9969, E-ISSN 1879-1506, Vol. 70, p. 1-8Article in journal (Refereed)
Abstract [en]

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.

Place, publisher, year, edition, pages
Elsevier, 2016. Vol. 70, p. 1-8
Keywords [en]
Host-pathogen interaction, Mucosal immunology, Protease inhibitor, Plasminogen activator inhibitor type 2, PAI-2, SerpinB2
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:mau:diva-5869DOI: 10.1016/j.archoralbio.2016.05.016ISI: 000385328100001PubMedID: 27295389Scopus ID: 2-s2.0-84979255164Local ID: 23310OAI: oai:DiVA.org:mau-5869DiVA, id: diva2:1402738
Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2024-06-17Bibliographically approved

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Publisher's full textPubMedScopushttp://www.sciencedirect.com/science/article/pii/S0003996916301261

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Neilands, JessicaKinnby, Bertil

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