ArticleJournal of bacteriology1997
Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membrane.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Syphilis vaccine: challenges, controversies and opportunities.Frontiers in immunology · 2023Review
- Analysis of host cell binding specificity mediated by the Tp0136 adhesin of the syphilis agent Treponema pallidum subsp. pallidum.PLoS neglected tropical diseases · 2019Article
- Functional clues from the crystal structure of an orphan periplasmic ligand-binding protein from Treponema pallidum.Protein science : a publication of the Protein Society · 2017Article
- Treponema pallidum Lipoprotein TP0435 Expressed in Borrelia burgdorferi Produces Multiple Surface/Periplasmic Isoforms and mediates Adherence.Scientific reports · 2016Article
- Structural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.Journal of bacteriology · 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
- Molecular structure and peptidoglycan recognition of Mycobacterium tuberculosis ArfA (Rv0899).Journal of molecular biology · 2012Article
- TP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane protein.Molecular microbiology · 2011Article
- Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum.Infection and immunity · 2010Article
- Mycobacterium tuberculosis Rv0899 adopts a mixed alpha/beta-structure and does not form a transmembrane beta-barrel.Biochemistry · 2010Article
- Assessment of cell-surface exposure and vaccinogenic potentials of Treponema pallidum candidate outer membrane proteins.Microbes and infection · 2007Article
- Quantitative assessment of protection in experimental syphilis.Infection and immunity · 2005Article
- TP0453, a concealed outer membrane protein of Treponema pallidum, enhances membrane permeability.Journal of bacteriology · 2005Article
- Molecular basis of bacterial outer membrane permeability revisited.Microbiology and molecular biology reviews : MMBR · 2003Review
- The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation.Journal of bacteriology · 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
- The tprK gene is heterogeneous among Treponema pallidum strains and has multiple alleles.Infection and immunity · 2000Article
- Renaturation of recombinant Treponema pallidum rare outer membrane protein 1 into a trimeric, hydrophobic, and porin-active conformation.Journal of bacteriology · 1999Article
- T-Cell responses to Treponema pallidum subsp. pallidum antigens during the course of experimental syphilis infection.Infection and immunity · 1999Article
- The Treponema denticola major sheath protein is predominantly periplasmic and has only limited surface exposure.Infection and immunity · 1999Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Treponema pallidum rare outer membrane protein 1 (Tromp1) has extensive sequence homology with substrate-binding proteins of ATP-binding cassette transporters. Because such proteins typically are periplasmic or cytoplasmic membrane associated, experiments were conducted to clarify Tromp1's physicochemical properties and cellular location in T. pallidum. Comparison of the sodium dodecyl sulfate-polyacrylamide gel electrophoresis mobilities of (i) native Tromp1 and Tromp1 synthesized by coupled in vitro transcription-translation and (ii) native Tromp1 and recombinant Tromp1 lacking the N-terminal signal sequence revealed that the native protein is not processed. Other studies demonstrated that recombinant Tromp1 lacks three basic porin-like properties: (i) the ability to form aqueous channels in liposomes which permit the influx of small hydrophilic solutes, (ii) an extensive beta-sheet secondary structure, and (iii) amphiphilicity. Subsurface localization of native Tromp1 was demonstrated by immunofluorescence analysis of treponemes encapsulated in gel microdroplets, while opsonization assays failed to detect surface-exposed Tromp1. Incubation of motile treponemes with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)-diazarine, a photoactivatable, lipophilic probe, also did not result in the detection of Tromp1 within the outer membranes of intact treponemes but, instead, resulted in the labeling of a basic 30.5-kDa presumptive outer membrane protein. Finally, analysis of fractionated treponemes revealed that native Tromp1 is associated predominantly with cell cylinders. These findings comprise a body of evidence that Tromp1 actually is anchored by an uncleaved signal sequence to the periplasmic face of the T. pallidum cytoplasmic membrane, where it likely subserves a transport-related function.
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What OpenQuestion holds
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.