Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola

Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of... 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 . http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biological Chemistry de Gruyter

Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola

Download PDF
9 pages

Loading next page...
 
/lp/de-gruyter/dentipain-a-streptococcus-pyogenes-ides-protease-homolog-is-a-novel-7Su0ICe1wO

References (43)

Publisher
de Gruyter
Copyright
©2010 by Walter de Gruyter Berlin New York
Subject
Protein Structure and Function
ISSN
1431-6730
eISSN
1437-4315
DOI
10.1515/BC.2010.113
pmid
20635859
Publisher site
See Article on Publisher Site

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 .

Journal

Biological Chemistry – de Gruyter

Published: Sep 1, 2010

Keywords: cysteine proteases; IgG-specific protease; immunoglobulin-like protein; oligopeptidase; periodontal diseases

There are no references for this article.