ArticleThe Journal of biological chemistry2013
Porphyromonas gingivalis virulence factor gingipain RgpB shows a unique zymogenic mechanism for cysteine peptidases.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- Mutagenesis and free energy calculations to optimize the ProRgpB inhibitor loop and identify variants with higher affinity forRSC advances · 2026Article
- Random Mutagenesis in Porphyromonas gingivalis Enables Isolation of Mutants With Enhanced Secreted Protease Activity.Molecular oral microbiology · 2026Article
- Oxysulfur and organosulfur toxins: the hidden mediators of the oral-systemic connection.Frontiers in microbiology · 2026Article
- Discovery of Gingipains andFoods (Basel, Switzerland) · 2025Review
- Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025Review
- Ecological, beneficial, and pathogenic functions of the Type 9 Secretion System.Microbial biotechnology · 2024Review
- A journey with type IX secretion system effectors: selection, transport, processing and activities.Microbiology (Reading, England) · 2023Article
- Implications ofFrontiers in cellular and infection microbiology · 2022Review
- Tetrahydroimidazo[4,5-Pharmaceuticals (Basel, Switzerland) · 2021Article
- Intermolecular latency regulates the essential C-terminal signal peptidase and sortase of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mechanisms Applied by Protein Inhibitors to Inhibit Cysteine Proteases.International journal of molecular sciences · 2021Review
- Bacterial Manipulation of the Integrated Stress Response: A New Perspective on Infection.Frontiers in microbiology · 2021Review
- Identification and Modification ofFrontiers in immunology · 2020Article
- Proteolytic processing and activation of gingipain zymogens secreted by T9SS of Porphyromonas gingivalis.Biochimie · 2019Article
- Pathogenesis of Important Virulence Factors ofFrontiers in cellular and infection microbiology · 2019Review
- Article
- Structural insights unravel the zymogenic mechanism of the virulence factor gingipain K fromThe Journal of biological chemistry · 2017Article
- The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain.Scientific reports · 2016Article
- Structure and mechanism of a bacterial host-protein citrullinating virulence factor, Porphyromonas gingivalis peptidylarginine deiminase.Scientific reports · 2015Article
- Purification and characterisation of recombinant His-tagged RgpB gingipain from Porphymonas gingivalis.Biological chemistry · 2015Article
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7 authors at 2 institutions in 3 countries.
Funding
Abstract
Zymogenicity is a regulatory mechanism that prevents inadequate catalytic activity in the wrong context. It plays a central role in maintaining microbial virulence factors in an inactive form inside the pathogen until secretion. Among these virulence factors is the cysteine peptidase gingipain B (RgpB), which is the major virulence factor secreted by the periodontopathogen Porphyromonas gingivalis that attacks host vasculature and defense proteins. The structure of the complex between soluble mature RgpB, consisting of a catalytic domain and an immunoglobulin superfamily domain, and its 205-residue N-terminal prodomain, the largest structurally characterized to date for a cysteine peptidase, reveals a novel fold for the prodomain that is distantly related to sugar-binding lectins. It attaches laterally to the catalytic domain through a large concave surface. The main determinant for latency is a surface "inhibitory loop," which approaches the active-site cleft of the enzyme on its non-primed side in a substrate-like manner. It inserts an arginine (Arg(126)) into the S1 pocket, thus matching the substrate specificity of the enzyme. Downstream of Arg(126), the polypeptide leaves the cleft, thereby preventing cleavage. Moreover, the carbonyl group of Arg(126) establishes a very strong hydrogen bond with the co-catalytic histidine, His(440), pulling it away from the catalytic cysteine, Cys(473), and toward Glu(381), which probably plays a role in orienting the side chain of His(440) during catalysis. The present results provide the structural determinants of zymogenic inhibition of RgpB by way of a novel inhibitory mechanism for peptidases in general and open the field for the design of novel inhibitory strategies in the treatment of human periodontal disease.
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