ArticleBiological chemistry2010
Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola.
Article in Biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Structural insights into the role of the prosegment binding loop in a papain-superfamily cysteine protease from Treponema denticola.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Treponema denticola major surface protein (Msp): a key player in periodontal pathogenicity and immune evasion.Archives of microbiology · 2025Review
- Innovative strategies targeting oral microbial dysbiosis: unraveling mechanisms and advancing therapies for periodontitis.Frontiers in cellular and infection microbiology · 2025Review
- Localization and pathogenic role of the cysteine protease dentipain in Treponema denticola.Molecular oral microbiology · 2023Article
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- A structure-derived snap-trap mechanism of a multispecific serpin from the dysbiotic human oral microbiome.The Journal of biological chemistry · 2017Article
- Linkages between oral commensal bacteria and atherosclerotic plaques in coronary artery disease patients.NPJ biofilms and microbiomes · 2016Article
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- Treponema denticola interactions with host proteins.Journal of oral microbiology · 2012Article
- Streptococcal IdeS and its impact on immune response and inflammation.Journal of innate immunity · 2012Review
- Diagnostic evaluation of a nanobody with picomolar affinity toward the protease RgpB from Porphyromonas gingivalis.Analytical biochemistry · 2011Article
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Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Treponema denticola is a major pathogen of chronic periodontitis. Analysis of the T. denticola genome revealed a gene orthologous with a cysteine protease-encoding gene from Streptococcus pyogenes (IdeS). IdeS interferes with IgG-dependent opsonophagocytosis by specific cleavage of IgG molecules. Analysis of this gene (termed ideT) 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 β-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 T. denticola.
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Registered trials
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