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, USA
  • Maryta Sztukowska, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, USA
  • Danuta Mizgalska, Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Polen
  • Mirosław Ksiazek, Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, USA
  • John Houston, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, USA
  • Barbara Potempa, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, USA
  • Jan Johannes Enghild
  • Ida B Thøgersen
  • F Xavier Gomis-Rüth, Proteolysis Lab, Molecular Biology Institute of Barcelona, Spanish Research Council CSIC, Spanien
  • Ky-Anh Nguyen, Institute of Dental Research, Westmead Centre for Oral Health and Westmead Millenium Institute, Australien
  • Jan Potempa, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, USA
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.
OriginalsprogEngelsk
TidsskriftBBA General Subjects
Vol/bind1830
Nummer8
Sider (fra-til)4218-4228
Antal sider11
ISSN0304-4165
DOI
StatusUdgivet - aug. 2013

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