ArticleInfection and immunity2008
A novel Treponema pallidum antigen, TP0136, is an outer membrane protein that binds human fibronectin.
Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed, 124 citations in OpenAlex.
- Putative mechanisms of ocular inflammation in syphilis.Journal of ophthalmic inflammation and infection · 2026Review
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- High quality transcriptome profiling confirms the transcriptional landscape of Treponema pallidum subsp. pallidum.Scientific reports · 2025Article
- Tp40: a new potential prognostic and diagnostic marker for syphilis.Microbiology spectrum · 2025Article
- Participants inFrontiers in immunology · 2025Review
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- Syphilis vaccine development: Aligning vaccine design with manufacturing requirements.Human vaccines & immunotherapeutics · 2024Article
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- Treponema pallidum Periplasmic and Membrane Proteins Are Recognized by Circulating and Skin CD4+ T Cells.The Journal of infectious diseases · 2024Article
- The hare syphilis agent is related to, but distinct from, the treponeme causing rabbit syphilis.PloS one · 2024Article
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- Advancements in the development of nucleic acid vaccines for syphilis prevention and control.Human vaccines & immunotherapeutics · 2023Review
- Immunization with Tp0954, an adhesin ofFrontiers in immunology · 2023Article
- Syphilis and the host: multi-omic analysis of host cellular responses toFrontiers in microbiology · 2023Article
- Syphilis vaccine: challenges, controversies and opportunities.Frontiers in immunology · 2023Review
- Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
The antigenicity, structural location, and function of the predicted lipoprotein TP0136 of Treponema pallidum subsp. pallidum were investigated based on previous screening studies indicating that anti-TP0136 antibodies are present in the sera of syphilis patients and experimentally infected rabbits. Recombinant TP0136 (rTP0136) protein was purified and shown to be strongly antigenic during human and experimental rabbit infection. The TP0136 protein was exposed on the surface of the bacterial outer membrane and bound to the host extracellular matrix glycoproteins fibronectin and laminin. In addition, the TP0136 open reading frame was shown to be highly polymorphic among T. pallidum subspecies and strains at the nucleotide and amino acid levels. Finally, the ability of rTP0136 protein to act as a protective antigen to subsequent challenge with infectious T. pallidum in the rabbit model of infection was assessed. Immunization with rTP0136 delayed ulceration but did not prevent infection or the formation of lesions. These results demonstrate that TP0136 is expressed on the outer membrane of the treponeme during infection and may be involved in attachment to host extracellular matrix components.
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Registered trials
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