ArticleThe Journal of biological chemistry2015
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.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- Navigating infection by pathogenic spirochetes: The host-bacteria interface at the atomic level.Protein science : a publication of the Protein Society · 2025Review
- Treponema denticola major surface protein (Msp): a key player in periodontal pathogenicity and immune evasion.Archives of microbiology · 2025Review
- In-Depth Proteome Coverage of In Vitro-CulturedJournal of proteome research · 2024Article
- Deep proteome coverage advances knowledge of Treponema pallidum protein expression profiles during infection.Scientific reports · 2023Article
- Advancements in the development of nucleic acid vaccines for syphilis prevention and control.Human vaccines & immunotherapeutics · 2023Review
- Review
- Syphilis vaccine: challenges, controversies and opportunities.Frontiers in immunology · 2023Review
- Full-length TprK of Treponema pallidum subsp. pallidum in lipid nanodiscs is a monomeric porin.Enzyme and microbial technology · 2022Article
- B-Cell Epitope Mapping of TprC and TprD Variants ofFrontiers in immunology · 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
- Article
- Evaluation of the Protective Ability of the Treponema pallidum subsp.Infection and immunity · 2019Article
- Complete genome sequences of two strains of Treponema pallidum subsp. pertenue from Indonesia: Modular structure of several treponemal genes.PLoS neglected tropical diseases · 2018Article
- Article
- The major outer sheath protein forms distinct conformers and multimeric complexes in the outer membrane and periplasm of Treponema denticola.Scientific reports · 2017Article
- Syphilis.Nature reviews. Disease primers · 2017Review
- Nanodiscs and Solution NMR: preparation, application and challenges.Nanotechnology reviews · 2017Article
- Vaccine development for syphilis.Expert review of vaccines · 2017Review
- NovelBioMed research international · 2017Review
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
We previously identified Treponema pallidum repeat proteins TprC/D, TprF, and TprI as candidate outer membrane proteins (OMPs) and subsequently demonstrated that TprC is not only a rare OMP but also forms trimers and has porin activity. We also reported that TprC contains N- and C-terminal domains (TprC(N) and TprC(C)) orthologous to regions in the major outer sheath protein (MOSP(N) and MOSP(C)) of Treponema denticola and that TprC(C) is solely responsible for β-barrel formation, trimerization, and porin function by the full-length protein. Herein, we show that TprI also possesses bipartite architecture, trimeric structure, and porin function and that the MOSP(C)-like domains of native TprC and TprI are surface-exposed in T. pallidum, whereas their MOSP(N)-like domains are tethered within the periplasm. TprF, which does not contain a MOSP(C)-like domain, lacks amphiphilicity and porin activity, adopts an extended inflexible structure, and, in T. pallidum, is tightly bound to the protoplasmic cylinder. By thermal denaturation, the MOSP(N) and MOSP(C)-like domains of TprC and TprI are highly thermostable, endowing the full-length proteins with impressive conformational stability. When expressed in Escherichia coli with PelB signal sequences, TprC and TprI localize to the outer membrane, adopting bipartite topologies, whereas TprF is periplasmic. We propose that the MOSP(N)-like domains enhance the structural integrity of the cell envelope by anchoring the β-barrels within the periplasm. In addition to being bona fide T. pallidum rare outer membrane proteins, TprC/D and TprI represent a new class of dual function, bipartite bacterial OMP.
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