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The role of the RgpA–Kgp proteinase–adhesin complexes in the adherence of Porphyromonas gingivalis to fibroblasts

¹ Cooperative Research Centre for Oral Health Science, School of Dental Science, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 720 Swanston Street, Victoria 3010, Australia
² Cooperative Research Centre for Chronic Inflammatory Diseases, Department of Medicine, The University of Melbourne, Melbourne, Victoria, Australia

Correspondence
Eric C. Reynolds
e.reynolds{at}unimelb.edu.au

Porphyromonas gingivalis strains W50 and ATCC 33277 were shown to bind to cultured human fibroblast (MRC-5) cells using flow cytometry. As the concentration of P. gingivalis strain W50 cells was increased relative to the concentration of MRC-5 cells, the number of W50 cells bound per MRC-5 cell increased, as did the percentage of MRC-5 cells with bacteria bound. However, this relationship was only seen for P. gingivalis strain ATCC 33277 at low cell concentrations: at high bacterial cell concentrations strain ATCC 33277 auto-aggregated and binding to the MRC-5 cells decreased. Strain W50 was therefore chosen to study the role of the surface proteinase–adhesin complexes (RgpA–Kgp complexes) in binding to MRC-5 cells. P. gingivalis W50 cells treated with an inhibitor of the RgpA–Kgp complexes exhibited reduced binding to MRC-5 cells. The purified active and proteinase-inactive RgpA–Kgp complexes competitively inhibited binding of W50 to MRC-5 cells, and isogenic mutants of W50 lacking RgpA/B and Kgp displayed reduced binding. P. gingivalis W50 mutant cells lacking Kgp exhibited the lowest binding to MRC-5 cells, suggesting an important role for this proteinase and its associated adhesins in binding to fibroblasts.