ArticleMolecular microbiology2011
TP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane protein.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 77 citations in OpenAlex.
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- Treponema denticola major surface protein (Msp): a key player in periodontal pathogenicity and immune evasion.Archives of microbiology · 2025Review
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- The Significance of the Cell-Mediated Host Immune Response in Syphilis.Microorganisms · 2024Review
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- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- In-Depth Proteome Coverage of In Vitro-CulturedJournal of proteome research · 2024Article
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- Deep proteome coverage advances knowledge of Treponema pallidum protein expression profiles during infection.Scientific reports · 2023Article
- Use of Epivolve phage display to generate a monoclonal antibody with opsonic activity directed against a subdominant epitope on extracellular loop 4 ofFrontiers in immunology · 2023Article
- Syphilis vaccine: challenges, controversies and opportunities.Frontiers in immunology · 2023Review
- Characterization of Treponema denticola Major Surface Protein (Msp) by Deletion Analysis and Advanced Molecular Modeling.Journal of bacteriology · 2022Article
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- Treponema pallidum genome sequencing from six continents reveals variability in vaccine candidate genes and dominance of Nichols clade strains in Madagascar.PLoS neglected tropical diseases · 2021Article
- Priorities for sexually transmitted infection vaccine research and development: Results from a survey of global leaders and representatives.Vaccine: X · 2021Article
- 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
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
Abstract
Definitive identification of Treponema pallidum rare outer membrane proteins (OMPs) has long eluded researchers. TP0326, the sole protein in T. pallidum with sequence homology to a Gram-negative OMP, belongs to the BamA family of proteins essential for OM biogenesis. Structural modelling predicted that five polypeptide transport-associated (POTRA) domains comprise the N-terminus of TP0326, while the C-terminus forms an 18-stranded amphipathic β-barrel. Circular dichroism, heat modifiability by SDS-PAGE, Triton X-114 phase partitioning and liposome incorporation supported these topological predictions and confirmed that the β-barrel is responsible for the native protein's amphiphilicity. Expression analyses revealed that native TP0326 is expressed at low abundance, while a protease-surface accessibility assay confirmed surface exposure. Size-exclusion chromatography and blue native polyacrylamide gel electrophoresis revealed a modular Bam complex in T. pallidum larger than that of Escherichia coli. Non-orthologous ancillary factors and self-association of TP0326 via its β-barrel may both contribute to the Bam complex. T. pallidum-infected rabbits mount a vigorous antibody response to both POTRA and β-barrel portions of TP0326, whereas humans with secondary syphilis respond predominantly to POTRA. The syphilis spirochaete appears to have devised a stratagem for harnessing the Bam pathway while satisfying its need to limit surface antigenicity.
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