View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Digital.CSIC Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases Florian Veillard1,#, Maryta Sztukowska1,#, Danuta Mizgalska2, Miros!aw Ksiazek2, John Houston1, Barbara Potempa1, Jan J. Enghild3, Ida B. Thogersen3, F. Xavier Gomis-Rüth4, Ky-Anh Nguyen5,6, Jan Potempa1,2,* 1Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY 40202, USA; e-mails:
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[email protected] 2Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. e-mails:
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[email protected] 3Center for Insoluble Protein Structures (inSPIN) and Interdisciplinary Nanoscience Center (iNANO) at the Department of Molecular Biology and Genetics, Aarhus University, Aarhus DK- 8000, Denmark; e-mails:
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[email protected] 4Proteolysis Lab, Molecular Biology Institute of Barcelona, Spanish Research Council CSIC, Barcelona Science Park, c/Baldiri Reixac 15-21, 08028 Barcelona, Catalonia (Spain); e-mail:
[email protected] 5Institute of Dental Research, Westmead Centre for Oral Health and Westmead Millenium Institute, Sydney NSW 2145, Australia; e-mail:
[email protected] 6Faculty of Dentistry, University of Sydney, Sydney NSW 2006, Australia. #These authors contributed equally to this study and share first authorship. *Corresponding author phone number: (+1) 502-852-1319 Abbreviations: PD, N-terminal prodomain; CD, catalytic domain; CTD, C-terminal domain ABSTRACT Background: 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.