{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T16:30:59Z","timestamp":1762101059929},"reference-count":39,"publisher":"Walter de Gruyter GmbH","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,9,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>Treponema denticola<\/jats:italic>is a major pathogen of chronic periodontitis. Analysis of the<jats:italic>T. denticola<\/jats:italic>genome revealed a gene orthologous with a cysteine protease-encoding gene from<jats:italic>Streptococcus pyogenes<\/jats:italic>(IdeS). IdeS interferes with IgG-dependent opsonophagocytosis by specific cleavage of IgG molecules. Analysis of this gene (termed<jats:italic>ideT<\/jats:italic>) revealed it to encode a two-domain protein whose N-terminus is composed of tandem immunoglobulin-like domains followed by a C-terminal IdeS-like protease domain. In this study we show that during secretion the IdeT protein is processed into an N-terminal fragment which remains associated with the cell, and a C-terminal part released into the medium. Although the secreted domain of IdeT, termed dentipain, shows only 25% identity to the IdeS protease, the putative catalytic cysteine and histidine residues are strongly conserved. Recombinant dentipain cleaves the insulin \u03b2-chain, an activity which is inhibited by E-64, a diagnostic inhibitor of cysteine proteases. Apart from insulin no cleavage of other protein substrates was detected, suggesting that dentipain has oligopeptidase activity. A mutant strain was constructed expressing a modified IdeT variant, the dentipain domain of which was deleted. This strain was found to be significantly reduced in its abscess-forming activity compared with the parental strain in a murine abscess model, suggesting that dentipain contributes to the virulence of<jats:italic>T. denticola<\/jats:italic>.<\/jats:p>","DOI":"10.1515\/bc.2010.113","type":"journal-article","created":{"date-parts":[[2010,7,16]],"date-time":"2010-07-16T15:41:52Z","timestamp":1279294912000},"source":"Crossref","is-referenced-by-count":18,"title":["Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola"],"prefix":"10.1515","volume":"391","author":[{"given":"Kazuyuki","family":"Ishihara","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katarzyna","family":"Wawrzonek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lindesey N.","family":"Shaw","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Satoru","family":"Inagaki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Meguru","family":"Miyamoto","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jan","family":"Potempa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"374","reference":[{"key":"p_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M410698200"},{"key":"p_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2005.10.012"},{"key":"p_3","doi-asserted-by":"publisher","DOI":"10.1111\/j.1600-0765.1986.tb01452.x"},{"key":"p_4","doi-asserted-by":"crossref","first-page":"18896","DOI":"10.1016\/S0021-9258(19)37045-0","volume":"267","author":"Chen Z.","year":"1992","journal-title":"J. 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