ArticleThe Journal of experimental medicine2001
The TprK protein of Treponema pallidum is periplasmic and is not a target of opsonic antibody or protective immunity.
Article in The Journal of experimental medicine, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
51 citing papers in PubMed, 71 citations in OpenAlex.
- Article
- Comprehensive Overview ofCurrent protein & peptide science · 2024Review
- Insights into the protective immune response by immunization with full-length recombinant TprK protein: cellular and humoral responses.NPJ vaccines · 2023Article
- Treponema pallidum subsp. pallidum with an Artificially impaired TprK antigenic variation system is attenuated in the Rabbit model of syphilis.PLoS pathogens · 2023Article
- Syphilis vaccine: challenges, controversies and opportunities.Frontiers in immunology · 2023Review
- Identification of a Potential Vaccine againstVaccines · 2022Article
- Article
- Evaluation of the Protective Ability of the Treponema pallidum subsp.Infection and immunity · 2019Article
- Insights into the genetic variation profile of tprK in Treponema pallidum during the development of natural human syphilis infection.PLoS neglected tropical diseases · 2019Article
- Profile of the tprK gene in primary syphilis patients based on next-generation sequencing.PLoS neglected tropical diseases · 2019Article
- Syphilis.Nature reviews. Disease primers · 2017Review
- A defined syphilis vaccine candidate inhibits dissemination of Treponema pallidum subspecies pallidum.Nature communications · 2017Article
- Vaccine development for syphilis.Expert review of vaccines · 2017Review
- Differential Growth ofFrontiers in 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
- A Homology Model Reveals Novel Structural Features and an Immunodominant Surface Loop/Opsonic Target in the Treponema pallidum BamA Ortholog TP_0326.Journal of bacteriology · 2015Article
- 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
- 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
- Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The finding that Treponema pallidum, the syphilis spirochete, contains 12 orthologs of the Treponema denticola outer membrane major sheath protein has engendered speculation that members of this T. pallidum repeat (Tpr) family may be similarly surface exposed. In this regard, the TprK protein was reported to be a target of opsonic antibody and protective immunity and subject to immunologically driven sequence variation. Despite these findings, results from our previous analyses of treponemal outer membranes in concert with computer-based predictions for TprK prompted us to examine the cellular location of this protein. TprK-alkaline phosphatase fusions expressed in Escherichia coli demonstrate that TprK contains a signal peptide. However, opsonophagocytosis assays failed to indicate surface exposure of TprK. Moreover, results from three independent methodologies, i.e., (a) indirect immunofluorescence analysis of agarose-encapsulated organisms, (b) proteinase K treatment of intact spirochetes, and (c) Triton X-114 phase partitioning of T. pallidum conclusively demonstrated that native TprK is entirely periplasmic. Consistent with this location, immunization with the recombinant protein failed to induce either protective immunity or select for TprK variants in the rabbit model of experimental syphilis. These findings challenge the notion that TprK will be a component of an efficacious syphilis vaccine.
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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.