ArticleJournal of bacteriology2013
The major outer sheath protein (Msp) of Treponema denticola has a bipartite domain architecture and exists as periplasmic and outer membrane-spanning conformers.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Expanded Functional Characterization and Optimization of Protein Expression in Treponema denticola Shuttle Plasmids.Molecular oral microbiology · 2026Article
- Navigating infection by pathogenic spirochetes: The host-bacteria interface at the atomic level.Protein science : a publication of the Protein Society · 2025Review
- Topology and functional characterization of major outer membrane proteins of Treponema maltophilum and Treponema lecithinolyticum.Molecular oral microbiology · 2025Article
- A bipartite bacterial virulence factor targets the complement system and neutrophil activation.The EMBO journal · 2025Article
- Treponema denticola major surface protein (Msp): a key player in periodontal pathogenicity and immune evasion.Archives of microbiology · 2025Review
- Characterization of Treponema denticola Major Surface Protein (Msp) by Deletion Analysis and Advanced Molecular Modeling.Journal of bacteriology · 2022Article
- Structural Modeling of the Treponema pallidum Outer Membrane Protein Repertoire: a Road Map for Deconvolution of Syphilis Pathogenesis and Development of a Syphilis Vaccine.Journal of bacteriology · 2021Article
- Putative β-Barrel Outer Membrane Proteins of the Bovine Digital Dermatitis-Associated Treponemes: Identification, Functional Characterization, and Immunogenicity.Infection and immunity · 2020Article
- Roles of TroA and TroR in Metalloregulated Growth and Gene Expression inJournal of bacteriology · 2020Article
- The Msp Protein of Treponema denticola Interrupts Activity of Phosphoinositide Processing in Neutrophils.Infection and immunity · 2019Article
- Immunotopological Analysis of theJournal of bacteriology · 2019Article
- Article
- 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
- A novel glycan modifies the flagellar filament proteins of the oral bacterium Treponema denticola.Molecular microbiology · 2017Article
- Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen.Nature reviews. Microbiology · 2016Review
- Genome-scale analysis of the non-cultivable Treponema pallidum reveals extensive within-patient genetic variation.Nature microbiology · 2016Article
- Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAIN.The Journal of biological chemistry · 2015Article
- Evidence that TP_0144 of Treponema pallidum is a thiamine-binding protein.Journal of bacteriology · 2015Article
- Structural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.Journal of bacteriology · 2014Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The major outer sheath protein (Msp) is a primary virulence determinant in Treponema denticola, as well as the parental ortholog for the Treponema pallidum repeat (Tpr) family in the syphilis spirochete. The Conserved Domain Database (CDD) server revealed that Msp contains two conserved domains, major outer sheath protein(N) (MOSP(N)) and MOSP(C), spanning residues 77 to 286 and 332 to 543, respectively, within the N- and C-terminal regions of the protein. Circular dichroism (CD) spectroscopy, Triton X-114 (TX-114) phase partitioning, and liposome incorporation demonstrated that full-length, recombinant Msp (Msp(Fl)) and a recombinant protein containing MOSP(C), but not MOSP(N), form amphiphilic, β-sheet-rich structures with channel-forming activity. Immunofluorescence analysis of intact T. denticola revealed that only MOSP(C) contains surface-exposed epitopes. Data obtained using proteinase K accessibility, TX-114 phase partitioning, and cell fractionation revealed that Msp exists as distinct OM-integrated and periplasmic trimers. Msp(Fl) folded in Tris buffer contained slightly less β-sheet structure than detergent-folded Msp(Fl); both forms, however, partitioned into the TX-114 detergent-enriched phase. CDD analysis of the nine Tpr paralogs predicted to be outer membrane proteins (OMPs) revealed that seven have an Msp-like bipartite structure; phylogenetic analysis revealed that the MOSP(N) and MOSP(C) domains of Msp are most closely related to those of TprK. Based upon our collective results, we propose a model whereby a newly exported, partially folded intermediate can be either processed for OM insertion by the β-barrel assembly machinery (BAM) or remain periplasmic, ultimately forming a stable, water-soluble trimer. Extrapolated to T. pallidum, our model enables us to explain how individual Tprs can localize to either the periplasmic (e.g., TprK) or OM (e.g., TprC) compartments.
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