ArticleBiological chemistry2009
Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage.
Article in Biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Comparison of gingival crevicular fluid sampling methods in patients with severe chronic periodontitis.Journal of periodontology · 2011Trial
- The protease code of the bacterial gut microbiota: ecological regulation, barrier disruption, and rewiring host defense and signaling.Gut microbes · 2026Review
- Matrix Metalloproteinases in the Periodontium-Vital in Tissue Turnover and Unfortunate in Periodontitis.International journal of molecular sciences · 2024Review
- Gingipains of Porphyromonas gingivalis Affect the Stability and Function of Serine Protease Inhibitor of Kazal-type 6 (SPINK6), a Tissue Inhibitor of Human Kallikreins.The Journal of biological chemistry · 2016Article
- The solution structure of the kallikrein-related peptidases inhibitor SPINK6.Biochemical and biophysical research communications · 2016Article
- A functional variant of elafin with improved anti-inflammatory activity for pulmonary inflammation.Molecular therapy : the journal of the American Society of Gene Therapy · 2015Article
- Periodontal treatment downregulates protease-activated receptor 2 in human gingival crevicular fluid cells.Infection and immunity · 2013Article
- Cleavage of IgG1 in gingival crevicular fluid is associated with the presence of Porphyromonas gingivalis.Journal of periodontal research · 2013Article
- Protease inhibitor levels in periodontal health and disease.Journal of periodontal research · 2012Article
- Periodontal pathogens affect the level of protease inhibitors in gingival crevicular fluid.Molecular oral microbiology · 2012Article
- Diagnostic evaluation of a nanobody with picomolar affinity toward the protease RgpB from Porphyromonas gingivalis.Analytical biochemistry · 2011Article
- Gingipains from Porphyromonas gingivalis - Complex domain structures confer diverse functions.European journal of microbiology & immunology · 2011Review
- Adsorption of components of the plasma kinin-forming system on the surface of Porphyromonas gingivalis involves gingipains as the major docking platforms.Infection and immunity · 2011Article
- Determinants of affinity and proteolytic stability in interactions of Kunitz family protease inhibitors with mesotrypsin.The Journal of biological chemistry · 2010Article
- Dichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins.Periodontology 2000 · 2010Review
- Functional study of elafin cleaved by Pseudomonas aeruginosa metalloproteinases.Biological chemistry · 2010Article
- Differential effects of periopathogens on host protease inhibitors SLPI, elafin, SCCA1, and SCCA2.Journal of oral microbiology · 2010Article
- A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037.Biological chemistry · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Abstract Porphyromonas gingivalis, the major causative bacterium of periodontitis, contributes significantly to elevated proteolytic activity at periodontal pockets owing to the presence of both bacteria and host, predominantly neutrophil-derived, serine proteases. Normally the activity of the latter enzymes is tightly regulated by endogenous proteins, including elafin, a potent neutrophil elastase and proteinase 3 inhibitor released from epithelial cells at sites of inflammation. Here, we report that all three gingipains (HRgpA, RgpB, and Kgp) have the ability to degrade elafin, with RgpB being far more efficient than other gingipains. RgpB efficiently inactivates the inhibitory activity of elafin at subnanomolar concentrations through proteolysis limited to the Arg22-Cys23 peptide bond within the surface loop harboring the inhibitor active site. Notably, elafin resists inactivation by several Staphylococcus aureus-derived serine and cysteine proteases, confirming the high stability of this protein against proteolytic degradation. Therefore, we conclude that elafin inactivation by RgpB represents a specific pathogenic adaptation of P. gingivalis to disturb the protease-protease inhibitor balance in the infected gingival tissue. This contributes to enhanced degradation of host proteins and generation of a pool of peptides serving as nutrients for this asaccharolytic pathogen.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.