RESUMEN
A 65 kDa protease was partially purified from extracellular vesicles of Fusobacterium nucleatum cultures by preparative SDS-PAGE followed by electroelution. The pH optimum of the protease is 7.5-8.0 and its activity could be inhibited by serine protease inhibitors. The protease was found to degrade the extracellular matrix proteins fibrinogen and fibronectin as well as collagen I and collagen IV which were degraded at 37 degrees C but not at 28 degrees C, indicating the presence of a gelatinase activity in these bacteria. The 65 kDa protease was also able to digest the alpha-chains of immunoglobulin A but not immunoglobulin G. The 65 kDa F. nucleatum protease, capable of degrading native proteins, may play an important role in both the nutrition and pathogenicity of these periodontal microorganisms. The degradation of extracellular matrix proteins by bacterial enzymes may contribute to the damage of periodontal tissues, and degradation of IgA may help the evasion of the immune system of the host by the bacteria.
