ArticleBiochimica et biophysica acta2013
Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases.
Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 28 citations in OpenAlex.
- Article
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- Proteolytic Activity Inhibition in Gingival Fluid by Cysteine Protease Inhibitors Obtained from Egg White andBiomedicines · 2025Article
- Limited proteolysis of neutrophil granule proteins by the bacterial protease RgpB depletes neutrophil antimicrobial capacity.Journal of leukocyte biology · 2025Article
- Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025Review
- Production and properties of adhesin-free gingipain proteinase RgpA.Scientific reports · 2023Article
- A journey with type IX secretion system effectors: selection, transport, processing and activities.Microbiology (Reading, England) · 2023Article
- Kgp DNA Vaccine Prevents Experimental Periodontitis.Oral health & preventive dentistry · 2021Article
- Phosphorylation of major Porphyromonas gingivalis virulence factors is crucial for their processing and secretion.Molecular oral microbiology · 2021Article
- Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogenJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Development of a novel, high-affinity ssDNA trypsin inhibitor.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Proteolytic processing and activation of gingipain zymogens secreted by T9SS of Porphyromonas gingivalis.Biochimie · 2019Article
- Maturation of the Mfa1 Fimbriae in the Oral PathogenFrontiers in cellular and infection microbiology · 2018Article
- Structural insights unravel the zymogenic mechanism of the virulence factor gingipain K fromThe Journal of biological chemistry · 2017Article
- Genes Contributing toFrontiers in cellular and infection microbiology · 2017Article
- Structural and functional probing of PorZ, an essential bacterial surface component of the type-IX secretion system of human oral-microbiomic Porphyromonas gingivalis.Scientific reports · 2016Article
- Noncanonical activation of β-catenin by Porphyromonas gingivalis.Infection and immunity · 2015Article
- Purification and characterisation of recombinant His-tagged RgpB gingipain from Porphymonas gingivalis.Biological chemistry · 2015Article
- Mirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia.Biological chemistry · 2015Article
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11 authors at 5 institutions in 6 countries.
Funding
Abstract
backgroundArginine-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.
methodsRecombinant forms of various prodomains (PD) were analyzed for their interaction with mature gingipains. The kinetics of their inhibition of proteolytic activity along with the formation of stable inhibitory complexes with native gingipains was studied by gel filtration, native PAGE and substrate hydrolysis.
resultsPDRgpB and PDRgpA formed tight complexes with arginine-specific gingipains (Ki in the range from 6.2nM to 0.85nM). In contrast, PDKgp showed no inhibitory activity. A conserved Arg-102 residue in PDRgpB and PDRgpA was recognized as the P1 residue. Mutation of Arg-102 to Lys reduced inhibitory potency of PDRgpB by one order of magnitude while its substitutions with Ala, Gln or Gly totally abolished the PD inhibitory activity. Covalent modification of the catalytic cysteine with tosyl-l-Lys-chloromethylketone (TLCK) or H-D-Phe-Arg-chloromethylketone did not affect formation of the stable complex.
conclusionLatency of arginine-specific progingipains is efficiently exerted by N-terminal prodomains thus protecting the periplasm from potentially damaging effect of prematurely activated gingipains. GENERAL SIGNIFICANCE: Blocking progingipain activation may offer an attractive strategy to attenuate P. gingivalis pathogenicity.
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