{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T14:06:04Z","timestamp":1787580364939,"version":"build-2736575974"},"reference-count":102,"publisher":"Walter de Gruyter GmbH","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n<jats:p>The genome of <jats:italic>Tannerella forsythia<\/jats:italic>, an etiological factor of chronic periodontitis, contains several genes encoding putative proteases. Here, we characterized a subtilisin-like serine protease of <jats:italic>T<\/jats:italic>. <jats:italic>forsythia<\/jats:italic> 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 <jats:italic>T. forsythia<\/jats:italic> pathogenicity by degradation of fibrinogen, hemoglobin, and the antimicrobial peptide LL-37.<\/jats:p>","DOI":"10.1515\/hsz-2014-0256","type":"journal-article","created":{"date-parts":[[2014,11,13]],"date-time":"2014-11-13T17:01:43Z","timestamp":1415898103000},"page":"261-275","source":"Crossref","is-referenced-by-count":33,"title":["Mirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia"],"prefix":"10.1515","volume":"396","author":[{"given":"Miroslaw","family":"Ksiazek","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abdulkarim Y.","family":"Karim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danuta","family":"Bryzek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan J.","family":"Enghild","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ida B.","family":"Th\u00f8gersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joanna","family":"Koziel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Potempa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","reference":[{"key":"ref361","first-page":"1","article-title":"Corruption of innate immunity by bacterial proteases","author":"Potempa","year":"2009","journal-title":"Innate Immun"},{"key":"ref901","first-page":"378","article-title":"and mapping of the active site of cysteine proteinases fromPorphyromonas gingivalis gingipains using peptidyl chloromethanes","author":"Potempa","year":"1997","journal-title":"Biol Chem"},{"key":"ref1041","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1111\/omi.12012","article-title":"Microbial interactions in building of communities Oral","volume":"28","author":"Wright","year":"2013","journal-title":"Mol Microbiol"},{"key":"ref461","doi-asserted-by":"publisher","DOI":"10.1111\/omi.12062","article-title":"The - layer proteins ofTannerella forsythiaare secreted via a type IX secretion system that is decoupled from proteinO - glycosylation Oral","author":"Tomek","year":"2014","journal-title":"Mol Microbiol"},{"key":"ref1011","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1902\/jop.2009.080532","article-title":"Gingival crevicular fluid levels of cathelicidin LL and interleukin in patients with chronic periodontitis","author":"T\u00fcrko\u011flu","year":"2009","journal-title":"Periodontol"},{"key":"ref401","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1128\/MMBR.62.3.597-635.1998","article-title":"Molecular and biotechnological aspects of microbial proteases","author":"Rao","year":"1998","journal-title":"Microbiol Mol Biol Rev"},{"key":"ref531","article-title":"Structural and functional analysis of the CspB protease required forClostridiumspore germination","author":"Adams","year":"2013","journal-title":"PLoS Pathog"},{"key":"ref781","first-page":"815","article-title":"Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes Protein","author":"Khan","year":"1998","journal-title":"Sci"},{"key":"ref751","first-page":"188","article-title":"metalloproteinase karilysin present in the majority ofTannerella forsythiaisolates inhibits all pathways of the complement system","author":"Jusko","year":"2012","journal-title":"Immunol"},{"key":"ref761","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1159\/000351458","article-title":"proteases aid in evasion of the human complement system","volume":"6","author":"Jusko","year":"2014","journal-title":"Innate Immun"},{"key":"ref861","doi-asserted-by":"publisher","DOI":"10.1111\/omi.12073[Epubaheadofprint]","article-title":"Suppression of inflammatory responses of human gingival fibroblasts by gingipains fromPorphyromonas gingivalis Oral Jul","volume":"23","author":"Palm","year":"2014","journal-title":"Mol Microbiol"},{"key":"ref201","first-page":"117","article-title":"Virulence factors of Treponema denticola","author":"Ishihara","year":"2010","journal-title":"Periodontol"},{"key":"ref671","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1111\/j.2041-1014.2012.00663.x","article-title":"Beyond the red complex and into more complexity : the polymicrobial synergy and dysbiosis model of periodontal disease etiology Oral","volume":"27","author":"Hajishengallis","year":"2012","journal-title":"Mol Microbiol"},{"key":"ref721","first-page":"160","article-title":"Proteases in bacterial pathogenesis","author":"Ingmer","year":"2009","journal-title":"Res Microbiol"},{"key":"ref921","first-page":"360","article-title":"Deficiency of antibacterial peptides in patients with morbus Kostmann an observation study","author":"P\u00fctsep","year":"2002","journal-title":"Lancet"},{"key":"ref591","first-page":"5","article-title":"New considerations in the prevalence of periodontal disease","author":"Fox","year":"1992"},{"key":"ref481","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1902\/jop.2009.080532","article-title":"Gingival crevicular fluid levels of cathelicidin LL and interleukin in patients with chronic periodontitis","author":"T\u00fcrko\u011flu","year":"2009","journal-title":"Periodontol"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1111\/j.1365-2958.2004.04276.x","article-title":"Calcium signalling in bacteria","author":"Dominguez","year":"2004","journal-title":"Mol Microbiol"},{"key":"ref181","first-page":"24800","article-title":"Strategies for the inhibition of gingipains for the potential treatment of periodontitis and associated systemic diseases Oral","author":"Ingar","year":"2014","journal-title":"Microbiol"},{"key":"ref431","first-page":"768","article-title":"Insights from bacterial subtilases into the mechanisms of intramolecular chaperone - 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terminal signal peptidase of a novel secretion system ofPorphyromonas gingivalis","author":"Glew","year":"2012","journal-title":"Biol Chem"},{"key":"ref711","first-page":"24800","article-title":"Strategies for the inhibition of gingipains for the potential treatment of periodontitis and associated systemic diseases Oral","author":"Ingar","year":"2014","journal-title":"Microbiol"},{"key":"ref801","first-page":"37","article-title":"Proteolytic inactivation of by karilysin a novel virulence mechanism ofTannerella forsythia","author":"Koziel","year":"2010","journal-title":"Innate Immun"},{"key":"ref341","first-page":"366","article-title":"Periodontal diseases","author":"Pihlstrom","year":"2005","journal-title":"Lancet"},{"key":"ref211","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/S0143416002001537","article-title":"Direct measurement of free Ca shows different regulation of Ca between the periplasm and the cytosol ofEscherichia coli","author":"Jones","year":"2002","journal-title":"Cell Calcium"},{"key":"ref231","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1159\/000351458","article-title":"proteases aid in evasion of the human complement system","volume":"6","author":"Jusko","year":"2014","journal-title":"Innate Immun"},{"key":"ref321","first-page":"67","article-title":"Offenbacher Periodontal infection as a possible risk factor for preterm low birth weight","author":"Katz","year":"1996","journal-title":"J Periodontol"},{"key":"ref931","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1128\/MMBR.62.3.597-635.1998","article-title":"Molecular and biotechnological aspects of microbial proteases","author":"Rao","year":"1998","journal-title":"Microbiol Mol Biol Rev"},{"key":"ref521","first-page":"712","article-title":"The lysine - 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operative haem acquisition by the HmuY haemophore ofPorphyromonas gingivalisand the cysteine protease interpain ofPrevotella intermedia Oral","volume":"28","author":"Byrne","year":"2013","journal-title":"Mol Microbiol"},{"key":"ref961","first-page":"768","article-title":"Insights from bacterial subtilases into the mechanisms of intramolecular chaperone - mediated activation of furin","author":"Shinde","year":"2011","journal-title":"Methods Mol Biol"},{"key":"ref1031","doi-asserted-by":"crossref","first-page":"4218","DOI":"10.1016\/j.bbagen.2013.04.005","article-title":"Inhibition of gingipains by their profragments as the mechanism protectingPorphyromonas gingivalisagainst premature activation of secreted proteases","author":"Veillard","year":"2013","journal-title":"Biochim Biophys Acta"},{"key":"ref501","doi-asserted-by":"crossref","first-page":"4218","DOI":"10.1016\/j.bbagen.2013.04.005","article-title":"Inhibition of gingipains by their profragments as the mechanism protectingPorphyromonas gingivalisagainst premature activation of secreted proteases","author":"Veillard","year":"2013","journal-title":"Biochim Biophys Acta"},{"key":"ref791","first-page":"351","article-title":"- armed bacteria in the skin","author":"Koziel","year":"2013","journal-title":"Cell Tissue Res"},{"key":"ref811","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1128\/JCM.30.2.427-433.1992","article-title":"Comparison of the benzoyl arginine - 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