Identification of a Fusobacterium nucleatum 65 kDa serine protease

G. Bachrach*, G. Rosen, M. Bellalou, R. Naor, Michael N. Sela

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


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°C but not at 28°C, indicating the presence of a gelatinase activity in these bacteria. The 65 kDa protease was also able to digest the α-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.

Original languageAmerican English
Pages (from-to)155-159
Number of pages5
JournalOral Microbiology and Immunology
Issue number3
StatePublished - Jun 2004


  • Extracellular matrix proteins
  • Extracellular vesicles
  • Fusobacteriuim nucleatum proteases


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