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

• Published in: Biochimica et biophysica acta Vol. 1830; no. 8; pp. 4218 - 4228
• Main Authors: Veillard, Florian, Sztukowska, Maryta, Mizgalska, Danuta, Ksiazek, Mirosław, Houston, John, Potempa, Barbara, Enghild, Jan J., Thogersen, Ida B., Gomis-Rüth, F. Xavier, Nguyen, Ky-Anh, Potempa, Jan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.08.2013
• Subjects: Adhesins, Bacterial - chemistry; Adhesins, Bacterial - drug effects; Adhesins, Bacterial - metabolism; cysteine; Cysteine Endopeptidases - chemistry; Cysteine Endopeptidases - drug effects; Cysteine Endopeptidases - metabolism; Cysteine Proteinase Inhibitors - pharmacology; cysteine proteinases; Enzyme Activation; gel chromatography; Glycosylation; hydrolysis; Inhibitor; mutation; Pathogen; Peptide Fragments - pharmacology; Periodontitis; polyacrylamide gel electrophoresis; Porphyromonas gingivalis; Porphyromonas gingivalis - pathogenicity; Protein Structure, Tertiary; proteolysis; Proteolysis control; Recombinant Proteins - pharmacology; secretion; virulence; Zymogen activation; zymogens; CD; CTD; Zymogen activation; PD; Periodontitis; Proteolysis control; Inhibitor; Pathogen

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 du...