Cloning, expression and purification of trypsin-like protease of the periodontal pathogen tannerella forsythia ATCC 43037

Abstract EN

Tannerella forsythia, a bacterial species frequently associated with the pathogenesis of periodontal disease and its proteases are implicated as virulence factors, is known to possess trypsin-like activity.

Here, we characterize a trypsin-like protease of T.

forsythia referred to as tlp.

Full length (without a signal peptide) recombinant tlp (102 kDa).

The evidence suggests that the enzyme is a serine protease since it was strongly inhibited by Pefabloc, Tosyl-L-Lysyl-chloromethane hydrochloride (TLCK) and Leupeptin.

The ability to degrade elastin, fibrinogen and the antimicrobial peptide LL-37 may contribute to the pathogenicity of periodontitis.