Summary auto-generated
This study examined how proteolytic enzymes from two major periodontal pathogens, Porphyromonas gingivalis and Treponema denticola, degrade host protease inhibitors and activate plasminogen. Researchers isolated an 80 kDa trypsin-like protease from P. gingivalis and a 95 kDa chymotrypsin-like protease from T. denticola, then tested their ability to break down six host protease inhibitors (α-1-antitrypsin, antichymotrypsin, α2-macroglobulin, antithrombin III, antiplasmin, and cystatin C). The P. gingivalis protease completely degraded all six inhibitors, while the T. denticola protease degraded most but was less effective against α2-macroglobulin and cystatin C. Among whole bacterial cells tested, P. gingivalis, T. denticola, Prevotella species, and Capnocytophaga showed significant degradative activity. The P. gingivalis protease demonstrated strong plasminogen activation capability, whereas the T. denticola protease did not. These findings suggest bacterial proteases contribute indirectly to periodontal tissue destruction by inactivating protective host defenses.
Key findings
- The 80 kDa protease from P. gingivalis completely degraded all six host protease inhibitors tested, while the 95 kDa protease from T. denticola was slightly less effective overall
- Among various oral bacterial species, P. gingivalis and T. denticola showed the most significant degradation of host protease inhibitors
- The 80 kDa protease from P. gingivalis strongly activated human plasminogen, whereas the 95 kDa protease from T. denticola showed no plasminogen activator activity
- Degradation of protease inhibitors by bacterial proteases may result in uncontrolled tissue destruction and rapid disease progression by reducing protective effects of these inhibitors
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Abstract
Bacterial proteases may participate in the pathogenesis of periodontal diseases through their action on host proteins. In the present study, the ability of selected periodontopathogens, as well as two proteases isolated from Porphyromonas gingivalis and Treponema denticola, to degrade host protease inhibitors was evaluated. The activation of human plasminogen by the two bacterial proteases was also investigated. Proteolytic breakdown of host protease inhibitors (alpha-1-antitrypsin, antichymotrypsin, alpha 2-macroglobulin, antithrombin III, antiplasmin and cystatin C) was evaluated by SDS-PAGE. The 80 kDa trypsin-like protease of P. gingivalis completely digested the six protease inhibitors under investigation, whereas the 95 kDa chymotrypsin-like protease of T. denticola was slightly less active, more particularly on alpha 2-macroglobulin and cystatin C. When whole cells from a number of oral bacterial species were tested, the most significant degradation was obtained with P. gingivalis, T. denticola, Prevotella intermedia, Prevotella nigrescens and Capnocytophaga spp. Peptostreptococcus micros and Propionibacterium acnes had only some degradative activity on selected inhibitors, whereas three bacterial species, Actinobacillus actinomycetemcomitans, Bacteroides forsythus and Fusobacterium nucleatum, had no effect on the protease inhibitors. The 80 kDa protease of P. gingivalis demonstrated strong plasminogen activation, whereas no such activity was associated with the 95 kDa protease of T. denticola. This study indicates the high potential of some periodontal pathogens to destroy protease inhibitors and activate plasminogen. This may result in an uncontrolled degradation of periodontal tissues and a rapid progression of the disease.