ArticleThe Journal of biological chemistry2014
Structure and mechanism of cysteine peptidase gingipain K (Kgp), a major virulence factor of Porphyromonas gingivalis in periodontitis.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.
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
59 citing papers in PubMed, 1 synthesis or guideline pooled it, 99 citations in OpenAlex.
- Assessment of the role of Trichomonas tenax in the etiopathogenesis of human periodontitis: A systematic review.PloS one · 2019Pooled it
- Interspecies regulation of virulence through gingipain inhibition by a Tannerella forsythia serpin.EMBO reports · 2026Article
- Testosterone Modulates Virulence-Associated Phenotypes ofPathogens (Basel, Switzerland) · 2026Article
- Heterogeneous Systemic IgG Responses to Porphyromonas gingivalis Gingipains in Advanced Periodontitis.Clinical and experimental dental research · 2026Article
- Article
- Virulence diversity amongJournal of oral microbiology · 2026Review
- The nasal-oral microbiome axis in allergic rhinitis: environmental triggers, microbial dysbiosis, and immune dysregulation.Frontiers in allergy · 2026Review
- Bacterial extracellular vesicles in the initiation, progression and treatment of atherosclerosis.Gut microbes · 2025Review
- Specialized shuttle proteins recognize Type IX secretion signals and target effectors to their final destinations in Flavobacterium johnsoniae.Communications biology · 2025Article
- Lys-specific gingipain (Kgp) ofmBio · 2025Article
- Discovery of Gingipains andFoods (Basel, Switzerland) · 2025Review
- Top-Down and Middle-Down Mass Spectrometry of Antibodies.Molecular & cellular proteomics : MCP · 2025Review
- Proteolytic Activity Inhibition in Gingival Fluid by Cysteine Protease Inhibitors Obtained from Egg White andBiomedicines · 2025Article
- Rapid detection of Lys-gingipain using fluorogenic peptide substrate for diagnosis of periodontitis.Journal of dental sciences · 2025Article
- Ozone ultrafine bubble water sterilizes Porphyromonas gingivalis and neutralizes its virulence factors.PloS one · 2025Article
- Synergistic effects ofFrontiers in cellular and infection microbiology · 2025Article
- Antibacterial Activity, Antiadherence Activity, Antioxidant Activity, and Molecular Docking of Sweetbrair Rose (Journal of pharmacy & bioallied sciences · 2024Article
- First crystal structure of the DUF2436 domain of virulence proteins from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Ecological, beneficial, and pathogenic functions of the Type 9 Secretion System.Microbial biotechnology · 2024Review
- Linking Periodontitis with Inflammatory Bowel Disease through the Oral-Gut Axis: The Potential Role ofBiomedicines · 2024Review
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 5 institutions in 4 countries.
Funding
Abstract
Cysteine peptidases are key proteolytic virulence factors of the periodontopathogen Porphyromonas gingivalis, which causes chronic periodontitis, the most prevalent dysbiosis-driven disease in humans. Two peptidases, gingipain K (Kgp) and R (RgpA and RgpB), which differ in their selectivity after lysines and arginines, respectively, collectively account for 85% of the extracellular proteolytic activity of P. gingivalis at the site of infection. Therefore, they are promising targets for the design of specific inhibitors. Although the structure of the catalytic domain of RgpB is known, little is known about Kgp, which shares only 27% sequence identity. We report the high resolution crystal structure of a competent fragment of Kgp encompassing the catalytic cysteine peptidase domain and a downstream immunoglobulin superfamily-like domain, which is required for folding and secretion of Kgp in vivo. The structure, which strikingly resembles a tooth, was serendipitously trapped with a fragment of a covalent inhibitor targeting the catalytic cysteine. This provided accurate insight into the active site and suggested that catalysis may require a catalytic triad, Cys(477)-His(444)-Asp(388), rather than the cysteine-histidine dyad normally found in cysteine peptidases. In addition, a 20-Å-long solvent-filled interior channel traverses the molecule and links the bottom of the specificity pocket with the molecular surface opposite the active site cleft. This channel, absent in RgpB, may enhance the plasticity of the enzyme, which would explain the much lower activity in vitro toward comparable specific synthetic substrates. Overall, the present results report the architecture and molecular determinants of the working mechanism of Kgp, including interaction with its substrates.
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.