Spirochetes at the forefront of periodontal infections

Ellen, Richard P.; Galimanas, Vaia B.

doi:10.1111/j.1600-0757.2005.00108.x

Cited by 154 publications

(149 citation statements)

References 180 publications

(275 reference statements)

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“…9,18,21,26 Recognizing the polymicrobial etiology of periodontitis, we compared the ability exerted by P. gingivalis to activate PAR 2 with the activity of T. denticola, an important periodontal pathogen that co-habits and forms biofilms with P. gingivalis and that also expresses proteinases with trypsin-like activity. 29,34 Unlike P. gingivalis, T. denticola culture supernatant did not activate PAR 2 , as it did not cause calcium signaling and did not desensitize PAR 2 activation by SLIGRL-NH 2 . Notably, both T. denticola outer membranes and its major outer sheath protein are known to cause calcium mobilization in fibroblasts, because of influx through the plasma membrane, but also to suppress subsequent agonist-induced calcium release from internal stores.…”

Section: Discussionmentioning

confidence: 99%

Protease-Activated Receptor-2 Activation

Holzhausen

Spolidorio

Ellen

et al. 2006

The American Journal of Pathology

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101

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We have investigated the specific contribution of protease-activated receptor-2 (PAR 2 ) to host defense during Porphyromonas gingivalis infection. Culture supernatants from P. gingivalis strains 33277 and W50 provoked Ca 2؉ mobilization in cells transfected with PAR 2 (PAR 2 -KNRK) and desensitized the subsequent responses to PAR 2 -selective agonist. In addition, culture supernatants of P. gingivalis E8 (RgpA/RgpB double knockout) did not cause calcium response in PAR 2 -KNRK cells, evidencing the involvement of the arginine-specific cysteine proteases RgpA and RgpB in PAR 2 activation by P. gingivalis. Injection of P. gingivalis into mouse subcutaneous chambers provoked an increased proteolytic activity, which was inhibited by serine protease inhibitors. Fluids collected from chambers of P. gingivalis-injected mice were able to activate PAR 2 and this activation was inhibited by serine protease inhibitors. P. gingivalis inoculation into subcutaneous chambers of wild-type mice induced an inflammatory response that was inhibited by a serine protease inhibitor and was significantly reduced in PAR 2 -deficient mice. Finally, mice orally challenged with P. gingivalis developed alveolar bone loss, which was significantly reduced in PAR 2 -deficient mice at 42 and 60 days after P. gingivalis infection. We conclude that PAR 2 is activated on P. gingivalis infection, in which it plays an important role in the host inflammatory response. (Am J Pathol

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Section: Discussionmentioning

confidence: 99%

Protease-Activated Receptor-2 Activation

Holzhausen

Spolidorio

Ellen

et al. 2006

The American Journal of Pathology

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101

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“…Treponema denticola is part of the microbiota of the human oral cavity and exists as part of a polymicrobial biofilm (subgingival dental plaque) accreted to the tooth root in the gingival crevice (Ellen & Galimanas, 2005). T. denticola, Porphyromonas gingivalis and Tannerella forsythia form a bacterial consortium that is strongly associated with the clinical progression of chronic periodontitis (Socransky et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Treponema denticola biofilm-induced expression of a bacteriophage, toxin–antitoxin systems and transposases

et al. 2010

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Treponema denticola is an oral spirochaete that has been strongly associated with chronic periodontitis. The bacterium exists as part of a dense biofilm (subgingival dental plaque) accreted to the tooth. To determine T. denticola gene products important for persistence as a biofilm we developed a continuous-culture biofilm model and conducted a genome-wide transcriptomic analysis of biofilm and planktonic cells. A total of 126 genes were differentially expressed with a fold change of 1.5 or greater. This analysis identified the upregulation of putative prophage genes in the T. denticola 35405 genome. Intact bacteriophage particles were isolated from T. denticola and circular phage DNA was detected by PCR analysis. This represents the first, to our knowledge, functional bacteriophage isolated from T. denticola, which we have designated Qtd1. In biofilm cells there was also an upregulation of genes encoding several virulence factors, toxinantitoxin systems and a family of putative transposases. Together, these data indicate that there is a higher potential for genetic mobility in T. denticola when growing as a biofilm and that these systems are important for the biofilm persistence and therefore virulence of this bacterium.

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“…In the healthy subgingival crevice, they account for ϳ1% of the total bacteria (5). With the progression of periodontitis, the abundance of oral treponemes increases dramatically and can reach 40% of the total bacterial population (6,7). Disease severity correlates specifically with the outgrowth of Treponema denticola and other bacterial species of the red microbial complex (6,8).…”

mentioning

confidence: 99%

Structure of Factor H-binding Protein B (FhbB) of the Periopathogen, Treponema denticola

Miller

Bell

McDowell

et al. 2012

Journal of Biological Chemistry

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Background:The Treponema denticola FhbB protein binds FH, a complement regulator. Results: The structure of FhbB was solved, and its interaction with FH was further defined. Conclusion: The structurally unique FhbB protein interacts with CCP7 of FH through electrostatic interactions. Significance: The T. denticola/FH interaction may perturb complement regulation resulting in conditions that favor the development of periodontal disease.

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Spirochetes at the forefront of periodontal infections

Cited by 154 publications

References 180 publications

Protease-Activated Receptor-2 Activation

Protease-Activated Receptor-2 Activation

Treponema denticola biofilm-induced expression of a bacteriophage, toxin–antitoxin systems and transposases

Structure of Factor H-binding Protein B (FhbB) of the Periopathogen, Treponema denticola

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