Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases

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  • Florian Veillard, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
  • Maryta Sztukowska, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
  • Danuta Mizgalska, Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Poland
  • Mirosław Ksiazek, Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, United States
  • John Houston, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
  • Barbara Potempa, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
  • Jan Johannes Enghild
  • Ida B Thøgersen
  • F Xavier Gomis-Rüth, Proteolysis Lab, Molecular Biology Institute of Barcelona, Spanish Research Council CSIC, Spain
  • Ky-Anh Nguyen, Institute of Dental Research, Westmead Centre for Oral Health and Westmead Millenium Institute, Australia
  • Jan Potempa, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
Arginine-specific (RgpB and RgpA) and lysine-specific (Kgp) gingipains are secretory cysteine proteinases of Porphyromonas gingivalis that act as important virulence factors for the organism. They are translated as zymogens with both N- and C-terminal extensions, which are proteolytically cleaved during secretion. In this report, we describe and characterize inhibition of the gingipains by their N-terminal prodomains to maintain latency during their export through the cellular compartments.
Original languageEnglish
JournalBBA General Subjects
Volume1830
Issue8
Pages (from-to)4218-4228
Number of pages11
ISSN0304-4165
DOIs
Publication statusPublished - Aug 2013

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