ArticleJournal of bacteriology1999
Physicochemical evidence that Treponema pallidum TroA is a zinc-containing metalloprotein that lacks porin-like structure.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Syphilis vaccine: challenges, controversies and opportunities.Frontiers in immunology · 2023Review
- Comparison of transcriptional profiles of Treponema pallidum during experimental infection of rabbits and in vitro culture: Highly similar, yet different.PLoS pathogens · 2021Article
- Biophysical insights into a highly selective l-arginine-binding lipoprotein of a pathogenic treponeme.Protein science : a publication of the Protein Society · 2018Article
- 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
- Manganese uptake and streptococcal virulence.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Review
- Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies.Frontiers in microbiology · 2015Review
- Varied metal-binding properties of lipoprotein PsaA in Streptococcus pneumoniae.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Halophilic properties of metal binding protein characterized by high histidine content from Chromohalobacter salexigens DSM3043.The protein journal · 2012Article
- Adaptation of Francisella tularensis to the mammalian environment is governed by cues which can be mimicked in vitro.Infection and immunity · 2008Article
- Assessment of cell-surface exposure and vaccinogenic potentials of Treponema pallidum candidate outer membrane proteins.Microbes and infection · 2007Article
- Biological basis for syphilis.Clinical microbiology reviews · 2006Review
- The Tp38 (TpMglB-2) lipoprotein binds glucose in a manner consistent with receptor function in Treponema pallidum.Journal of bacteriology · 2004Article
- 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 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
- The Treponema pallidum Outer Membrane.Current topics in microbiology and immunologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Although TroA (Tromp1) was initially reported to be a Treponema pallidum outer membrane protein with porin-like properties, subsequent studies have suggested that it actually is a periplasmic substrate-binding protein involved in the transport of metals across the treponemal cytoplasmic membrane. Here we conducted additional physicochemical studies to address the divergent viewpoints concerning this protein. Triton X-114 phase partitioning of recombinant TroA constructs with or without a signal sequence corroborated our prior contention that the native protein's amphiphilic behavior is due to its uncleaved leader peptide. Whereas typical porins are trimers with extensive beta-barrel structure, size exclusion chromatography and circular dichroism spectroscopy revealed that TroA was a monomer and predominantly alpha-helical. Neutron activation, atomic absorption spectroscopy, and anomalous X-ray scattering all demonstrated that TroA binds zinc in a 1:1 molar stoichiometric ratio. TroA does not appear to possess structural features consistent with those of bacterial porins.
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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.