Cloning, Expression and Purification of Trypsin-like Protease of the Periodontal Pathogen Tannerella forsythia ATCC 43037

Keywords: trypsin-like protease, cloning, periodontitis, protein expression


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.


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How to Cite
“Cloning, Expression and Purification of Trypsin-like Protease of the Periodontal Pathogen Tannerella forsythia ATCC 43037” (2018) Zanco Journal of Pure and Applied Sciences, 29(6), pp. 1-9. doi: 10.21271/ZJPAS.29.6.1.