Dipeptidyl peptidase-4 (DPP4), a non-specific, secreted protease with potential lipase properties, is thought be one of the first enzymes produced by pathogens in flesh-eating diseases. When DPP4 is secreted, it causes extensive tissue damage, which is the hallmark of flesh-eating disease. P. intermedia, a member of normal human oral flora and opportunistic pathogen in flesh-eating diseases, is believed to be a major contributor in DPP4 production. In an effort to understand this poorly characterized serine protease, we have cloned and expressed P. intermedia DPP4 in E. coli. Previous attempts to clone this enzyme have been unsuccessful due to problems with E. coli expression and enzyme solubility. We have worked around this problem by using a low concentration of urea to increase solubility, but not unfold the enzyme. The enzyme demonstrates activity toward other E. coli proteins and characterization has begun on the enzyme. This work will advance our understanding of secreted proteases produced by pathogens and could lead to the development of drugs to inhibit its protease activity, minimizing tissue damage in flesh-eating diseases.

Characterization of a robust serine protease from P. intermedia

253rd National Meeting (2017)

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