ArticleBiological chemistry2015
Mirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia.
Article in Biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 35 citations in OpenAlex.
- Genome-wide identification, characterization and expression analysis of the subtilisin-like protease gene family in Quercus ilex in response to Phytophthora cinnamomi.Scientific reports · 2026Article
- The biological control potential of extracellular protein from Bacillus velezensis against Ralstonia solanacearum in tomatoes.Archives of microbiology · 2026Article
- Microbial Coaggregation in the Oral Cavity: Molecular Interactions and Current Insights.International journal of molecular sciences · 2025Review
- Functional study of Bergeyella cardium KP-43 subfamily peptidases as putative T9SS cargo.Communications biology · 2025Article
- Serine protease RAYM_01812 (SspA) inhibits complement-mediated killing and monocyte chemotaxis and contributes to virulence ofVirulence · 2024Article
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- Riemerella anatipestifer T9SS Effector SspA Functions in Bacterial Virulence and Defending Natural Host Immunity.Applied and environmental microbiology · 2022Article
- Maturation of subtilisin-like protease NbSLP1 from microsporidiaFrontiers in cellular and infection microbiology · 2022Article
- Genome-wide analysis of the SBT gene family involved in drought tolerance in cotton.Frontiers in plant science · 2022Article
- 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
- Comparative proteomics ofOne health (Amsterdam, Netherlands) · 2021Article
- Gene Analysis, Cloning, and Heterologous Expression of Protease from a MicromyceteMicroorganisms · 2021Article
- Interactions Between Neutrophils and Periodontal Pathogens in Late-Onset Periodontitis.Frontiers in cellular and infection microbiology · 2021Review
- Adhesion of anaerobic periodontal pathogens to extracellular matrix proteins.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Review
- Article
- The role ofInfectious agents and cancer · 2019Review
- The contribution of Tannerella forsythia dipeptidyl aminopeptidase IV in the breakdown of collagen.Molecular oral microbiology · 2018Article
- In vivo expression of proteases and protease inhibitor, a serpin, by periodontal pathogens at teeth and implants.Molecular oral microbiology · 2018Article
- Sensitivity of Enzymatic Toxins from Corneal Isolate of Acanthamoeba Protozoan to Physicochemical Parameters.Current microbiology · 2017Article
- Tobacco phytaspase: Successful expression in a heterologous system.Bioengineered · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The genome of Tannerella forsythia, an etiological factor of chronic periodontitis, contains several genes encoding putative proteases. Here, we characterized a subtilisin-like serine protease of T. forsythia referred to as mirolase. Recombinant full-length latent promirolase [85 kDa, without its signal peptide (SP)] processed itself through sequential autoproteolytic cleavages into a mature enzyme of 40 kDa. Mirolase latency was driven by the N-terminal prodomain (NTP). In stark contrast to almost all known subtilases, the cleaved NTP remained non-covalently associated with mirolase, inhibiting its proteolytic, but not amidolytic, activity. Full activity was observed only after the NTP was gradually, and fully, degraded. Both activity and processing was absolutely dependent on calcium ions, which were also essential for enzyme stability. As a consequence, both serine protease inhibitors and calcium ions chelators inhibited mirolase activity. Activity assays using an array of chromogenic substrates revealed that mirolase specificity is driven not only by the substrate-binding subsite S1, but also by other subsites. Taken together, mirolase is a calcium-dependent serine protease of the S8 family with the unique mechanism of activation that may contribute to T. forsythia pathogenicity by degradation of fibrinogen, hemoglobin, and the antimicrobial peptide LL-37.
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