ArticleInfection and immunity1999
Membrane topology and cellular location of the Treponema pallidum glycerophosphodiester phosphodiesterase (GlpQ) ortholog.
Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
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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
24 citing papers in PubMed, 36 citations in OpenAlex.
- Review
- Syphilis vaccine: challenges, controversies and opportunities.Frontiers in immunology · 2023Review
- A defined syphilis vaccine candidate inhibits dissemination of Treponema pallidum subspecies pallidum.Nature communications · 2017Article
- Vaccine development for syphilis.Expert review of vaccines · 2017Review
- Antigenic variation of TprK facilitates development of secondary syphilis.Infection and immunity · 2014Article
- TprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structure.Journal of bacteriology · 2012Article
- The transition from closed to open conformation of Treponema pallidum outer membrane-associated lipoprotein TP0453 involves membrane sensing and integration by two amphipathic helices.The Journal of biological chemistry · 2011Article
- Bifunctional role of the Treponema pallidum extracellular matrix binding adhesin Tp0751.Infection and immunity · 2011Article
- Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum.Infection and immunity · 2010Article
- Pneumococcal Haemophilus influenzae protein D conjugate vaccine induces antibodies that inhibit glycerophosphodiester phosphodiesterase activity of protein D.Infection and immunity · 2008Article
- Reactivity of antibodies from syphilis patients to a protein array representing the Treponema pallidum proteome.Journal of clinical microbiology · 2006Article
- Biological basis for syphilis.Clinical microbiology reviews · 2006Review
- TP0453, a concealed outer membrane protein of Treponema pallidum, enhances membrane permeability.Journal of bacteriology · 2005Article
- Quantitative assessment of protection in experimental syphilis.Infection and immunity · 2005Article
- Phagocytosis of Treponema pallidum and reactive oxygen species production by isolated rat Kupffer cells.Medical microbiology and immunology · 2003Article
- Serodiagnosis of syphilis: antibodies to recombinant Tp0453, Tp92, and Gpd proteins are sensitive and specific indicators of infection by Treponema pallidum.Journal of clinical microbiology · 2003Article
- Systematic cloning of Treponema pallidum open reading frames for protein expression and antigen discovery.Genome research · 2003Article
- Glycerol-3-phosphate acquisition in spirochetes: distribution and biological activity of glycerophosphodiester phosphodiesterase (GlpQ) among Borrelia species.Journal of bacteriology · 2003Article
- Novel 45-kilodalton leptospiral protein that is processed to a 31-kilodalton growth-phase-regulated peripheral membrane protein.Infection and immunity · 2002Article
- The TprK protein of Treponema pallidum is periplasmic and is not a target of opsonic antibody or protective immunity.The Journal of experimental medicine · 2001Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Recent reports that isolated Treponema pallidum outer membranes contain an ortholog for glycerophosphodiester phosphodiesterase (GlpQ) (D. V. Shevchenko, D. R. Akins, E. J. Robinson, M. Li, O. V. Shevchenko, and J. D. Radolf, Infect. Immun. 65:4179-4189, 1997) and that this protein is a potential opsonic target for T. pallidum (C. E. Stebeck, J. M. Shaffer, T. W. Arroll, S. A. Lukehart, and W. C. Van Voorhis, FEMS Microbiol. Lett. 154:303-310, 1997) prompted a more detailed investigation of its physicochemical properties and cellular location. [14C]palmitate radiolabeling studies of a GlpQ-alkaline phosphatase fusion expressed in Escherichia coli confirmed the prediction from DNA sequencing that the protein is lipid modified. Studies using Triton X-114 phase partitioning revealed that the protein's amphiphilicity is due to lipid modification and that a substantial portion of the polypeptide is associated with the T. pallidum peptidoglycan sacculus. Three different approaches, i.e., (i) proteinase K treatment of intact treponemes, (ii) indirect immunofluorescence analysis of treponemes encapsulated in agarose beads, and (iii) opsonophagocytosis of treponemes incubated with antiserum against recombinant GlpQ by rabbit peritoneal macrophages, confirmed that GlpQ is entirely subsurface in T. pallidum. Moreover, rabbits hyperimmunized with GlpQ were not protected against intradermal challenge with virulent treponemes. Circular dichroism spectroscopy confirmed that the recombinant form of the polypeptide lacked discernible evidence of denaturation. Finally, GlpQ was not radiolabeled when T. pallidum outer membranes were incubated with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)-diazarene, a photoactivatable, lipophilic probe which promiscuously labels both proteins and lipids within phospholipid bilayers. Taken as a whole, these studies indicate that the T. pallidum GlpQ ortholog is a periplasmic protein associated predominantly with the spirochete's peptidoglycan-cytoplasmic membrane complex.
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