ArticleInfection and immunity2011
Composition and localization of Treponema denticola outer membrane complexes.
Article in Infection and immunity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed.
- Topology and functional characterization of major outer membrane proteins of Treponema maltophilum and Treponema lecithinolyticum.Molecular oral microbiology · 2025Article
- Treponema denticola major surface protein (Msp): a key player in periodontal pathogenicity and immune evasion.Archives of microbiology · 2025Review
- Purification of Native Dentilisin Complex fromBio-protocol · 2024Article
- Activation of bone marrow-derived dendritic cells and CD4Journal of oral microbiology · 2022Article
- Treponema denticola dentilisin triggered TLR2/MyD88 activation upregulates a tissue destructive program involving MMPs via Sp1 in human oral cells.PLoS pathogens · 2021Article
- Periodontal Pathogens' strategies disarm neutrophils to promote dysregulated inflammation.Molecular oral microbiology · 2021Review
- Approaches to Understanding Mechanisms of Dentilisin Protease Complex Expression inFrontiers in cellular and infection microbiology · 2021Review
- Investigation of the potential regulator proteins associated with the expression of major surface protein and dentilisin inJournal of oral microbiology · 2020Article
- Oral and intestinal bacterial exotoxins: Potential linked to carcinogenesis.Progress in molecular biology and translational science · 2020Review
- The Msp Protein of Treponema denticola Interrupts Activity of Phosphoinositide Processing in Neutrophils.Infection and immunity · 2019Article
- The major outer sheath protein forms distinct conformers and multimeric complexes in the outer membrane and periplasm of Treponema denticola.Scientific reports · 2017Article
- The C-terminal region of the major outer sheath protein of Treponema denticola inhibits neutrophil chemotaxis.Molecular oral microbiology · 2017Article
- Human neutrophils and oral microbiota: a constant tug-of-war between a harmonious and a discordant coexistence.Immunological reviews · 2016Review
- Treponema denticola upregulates MMP-2 activation in periodontal ligament cells: interplay between epigenetics and periodontal infection.Archives of oral biology · 2014Article
- Characterization of Treponema denticola mutants defective in the major antigenic proteins, Msp and TmpC.PloS one · 2014Article
- Conservation and revised annotation of the Treponema denticola prcB-prcA-prtP locus encoding the dentilisin (CTLP) protease complex.Molecular oral microbiology · 2013Article
- The major outer sheath protein (Msp) of Treponema denticola has a bipartite domain architecture and exists as periplasmic and outer membrane-spanning conformers.Journal of bacteriology · 2013Article
- Treponema denticola major outer sheath protein impairs the cellular phosphoinositide balance that regulates neutrophil chemotaxis.PloS one · 2013Article
- Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities.Microbiology (Reading, England) · 2012Article
- Development of a modified gentamicin resistance cassette for genetic manipulation of the oral spirochete Treponema denticola.Applied and environmental microbiology · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The Treponema denticola outer membrane lipoprotein-protease complex (dentilisin) contributes to periodontal disease by degrading extracellular matrix components and disrupting intercellular host signaling pathways. We recently demonstrated that prcB, located upstream of and cotranscribed with prcA and prtP, encodes a 22-kDa lipoprotein that interacts with PrtP and is required for its activity. Here we further characterize products of the protease locus and their roles in expression, formation, and localization of outer membrane complexes. PrcB migrates in native gels as part of a >400-kDa complex that includes PrtP and PrcA, as well as the major outer sheath protein Msp. PrcB is detectable as a minor constituent of the purified active protease complex, which was previously reported to consist of only PrtP and auxiliary polypeptides PrcA1 and PrcA2. Though it lacks the canonical ribosome binding site present upstream of both prcA and prtP, PrcB is present at levels similar to those of PrtP in whole-cell extracts. Immunofluorescence microscopy demonstrated cell surface exposure of the mature forms of PrtP, PrcA1, PrcB, and Msp. The 16-kDa N-terminal acylated fragment of PrtP (predicted to be released during activation of PrtP) was present in cell extracts but was detected neither in the purified active protease complex nor on the cell surface. PrcA2, detectable on the surface of Msp-deficient cells but not that of wild-type cells, coimmunoprecipitated with Msp. Our results indicate that PrcB is a component of the outer membrane lipoprotein protease complex and that Msp and PrcA2 interaction may mediate formation of a very-high-molecular-weight outer membrane complex.
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Registered trials
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