ArticleInfection and immunity1999
The Treponema denticola major sheath protein is predominantly periplasmic and has only limited surface exposure.
Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 43 citations in OpenAlex.
- Bactofilins are essential spatial organizers of peptidoglycan insertion in the Lyme disease spirocheteJournal of bacteriology · 2026Article
- Treponema denticola major surface protein (Msp): a key player in periodontal pathogenicity and immune evasion.Archives of microbiology · 2025Review
- Outer Membrane Vesicles Derived from Oral Bacteria Act as a Dagger in Host Immunity: Insight Tips from Local Diseases to Systemic Effects.International journal of biological sciences · 2025Review
- Oral and intestinal bacterial exotoxins: Potential linked to carcinogenesis.Progress in molecular biology and translational science · 2020Review
- Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts.Cell death and differentiation · 2018Article
- 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
- Article
- 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
- TprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structure.Journal of bacteriology · 2012Article
- Composition and localization of Treponema denticola outer membrane complexes.Infection and immunity · 2011Article
- Article
- The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis.BMC infectious diseases · 2010Article
- Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum.Infection and immunity · 2010Article
- Cryo-electron tomography elucidates the molecular architecture of Treponema pallidum, the syphilis spirochete.Journal of bacteriology · 2009Article
- Involvement of Toll-like receptors 2 and 4 in the innate immune response to Treponema denticola and its outer sheath components.Infection and immunity · 2009Article
- Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405.Infection and immunity · 2005Article
- Outer membrane proteins of pathogenic spirochetes.FEMS microbiology reviews · 2004Review
- The TprK protein of Treponema pallidum is periplasmic and is not a target of opsonic antibody or protective immunity.The Journal of experimental medicine · 2001Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The recent discovery that the Treponema pallidum genome encodes 12 orthologs of the Treponema denticola major sheath protein (Msp) prompted us to reexamine the cellular location and topology of the T. denticola polypeptide. Experiments initially were conducted to ascertain whether Msp forms an array on or within the T. denticola outer membrane. Transmission electron microscopy (EM) of negatively stained and ultrathin-sectioned organisms failed to identify a typical surface layer, whereas freeze-fracture EM revealed that the T. denticola outer membrane contains heterogeneous transmembrane proteins but no array. In contrast, a lattice-like structure was observed in vesicles released from mildly sonicated treponemes; combined EM and biochemical analyses demonstrated that this structure was the peptidoglycan sacculus. Immunoelectron microscopy (IEM) subsequently was performed to localize Msp in T. denticola. Examination of negatively stained whole mounts identified substantial amounts of Msp in sonicated organisms. IEM of ultrathin-sectioned, intact treponemes also demonstrated that the preponderance of antigen was unassociated with the outer membrane. Lastly, immunofluorescence analysis of treponemes embedded in agarose gel microdroplets revealed that only minor portions of Msp are surface exposed. Taken as a whole, our findings challenge the widely held belief that Msp forms an array within the T. denticola outer membrane and demonstrate, instead, that it is predominantly periplasmic with only limited surface exposure. These findings also have implications for our evolving understanding of the contribution(s) of Msp/Tpr orthologs to treponemal physiology and disease pathogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.