Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogen Tannerella forsythia

• Main Authors: Krzysztof M. Zak (Author), Mark J. Bostock (Author), Irena Waligorska (Author), Ida B. Thøgersen (Author), Jan J. Enghild (Author), Grzegorz M. Popowicz (Author), Przemyslaw Grudnik (Author), Jan Potempa (Author), Miroslaw Ksiazek (Author)
• Format: Book
• Published: Taylor & Francis Group, 2021-01-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

Mirolysin is a secretory protease of Tannerella forsythia, a member of the dysbiotic oral microbiota responsible for periodontitis. In this study, we show that mirolysin latency is achieved by a "cysteine-switch" mechanism exerted by Cys23 in the N-terminal profragment. Mutation of Cys23 s...