Characterization of the trypsin-like activity of Bacteroides forsythus

Article Abstract:

Bacteroides forsythus is implicated as part of periodontitis, but its role as agitator or secondary infective agent is unknown. The bacteria has an enzyme with activities similar to that of trypsin that responds to hydrolysis of larger proteins contained in other oral bacteria and a zwitterionic detergent. The enzyme is on the surface of the bacteria and is likely a serine protease because of its reaction to diisopropylfluorophosphate, a known serine protease inhibitor.

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A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins

Article Abstract:

The cell-associated trypsin-like proteinases of Porphyromonas gingivalis W50 were characterized. The PrtR-PrtK complex was found composed of two gene products namely, the mature PrtR (160 kDa) and mature PrtK (163 kDa) that were further proteolytically processed to release proteinase and adhesin domains that remain non-covalently associated. It was proposed that the proteinase-adhesin complex is a major virulence factor for P. gingivalis.

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Degradation of host protease inhibitors and activation of plasminogen by proteolytic enzymes from Porphyromonas gingivalis and Treponema denticola

Article Abstract:

The capability of certain periodontopathogens and two proteases from Porphyromonas gingivalis and Treponema denticola, to destroy host protease inhibitors was examined. Findings demonstrated the high potential of some periodontal pathogens to degrade protease inhibitors and activate plasminogen which may cause an uncontrolled deterioration of periodontal tissues and a fast progression of the disease.

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