ArticleProceedings of the National Academy of Sciences of the United States of America1994
The 47-kDa major lipoprotein immunogen of Treponema pallidum is a penicillin-binding protein with carboxypeptidase activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 42 citations in OpenAlex.
- Bright New Resources for Syphilis Research: Genetically Encoded Fluorescent Tags for Treponema pallidum and Sf1Ep Cells.Molecular microbiology · 2024Article
- Antimicrobial susceptibility of Treponema pallidum subspecies pallidum: an in-vitro study.The Lancet. Microbe · 2023Article
- A large screen identifies beta-lactam antibiotics which can be repurposed to target the syphilis agent.npj antimicrobials and resistance · 2023Article
- Article
- Characterizing the Syphilis-Causing Treponema pallidum ssp. pallidum Proteome Using Complementary Mass Spectrometry.PLoS neglected tropical diseases · 2016Article
- Macrolide Resistance in the Syphilis Spirochete, Treponema pallidum ssp. pallidum: Can We Also Expect Macrolide-Resistant Yaws Strains?The American journal of tropical medicine and hygiene · 2015Article
- The endemic treponematoses.Clinical microbiology reviews · 2014Review
- Global challenge of antibiotic-resistant Treponema pallidum.Antimicrobial agents and chemotherapy · 2010Review
- Biological basis for syphilis.Clinical microbiology reviews · 2006Review
- TP0453, a concealed outer membrane protein of Treponema pallidum, enhances membrane permeability.Journal of bacteriology · 2005Article
- The Tp38 (TpMglB-2) lipoprotein binds glucose in a manner consistent with receptor function in Treponema pallidum.Journal of bacteriology · 2004Article
- Characterization of the leptospiral outer membrane and description of three novel leptospiral membrane proteins.Infection and immunity · 2002Article
- New tests for syphilis: rational design of a PCR method for detection of Treponema pallidum in clinical specimens using unique regions of the DNA polymerase I gene.Journal of clinical microbiology · 2001Article
- Membrane topology and cellular location of the Treponema pallidum glycerophosphodiester phosphodiesterase (GlpQ) ortholog.Infection and immunity · 1999Article
- Evidence for a methyl-accepting chemotaxis protein gene (mcp1) that encodes a putative sensory transducer in virulent Treponema pallidum.Infection and immunity · 1997Article
- Characterization of outer membranes isolated from Treponema pallidum, the syphilis spirochete.Infection and immunity · 1995Article
- Membrane topology of Borrelia burgdorferi and Treponema pallidum lipoproteins.Infection and immunity · 1995Article
- Dermal inflammation elicited by synthetic analogs of Treponema pallidum and Borrelia burgdorferi lipoproteins.Infection and immunity · 1995Article
- The Treponema pallidum Outer Membrane.Current topics in microbiology and immunologyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The recent model of Treponema pallidum molecular architecture proposes that the vast majority of the bacterium's integral membrane proteins are lipoprotein immunogens anchored in the cytoplasmic membrane while the outer membrane contains only a limited number of surface-exposed transmembrane proteins. This unique model explains, in part, the organism's remarkable ability to evade host immune defenses and establish persistent infection. Our strategy for refining this model involves demonstrating that the physiological functions of treponemal membrane proteins are consistent with their proposed cellular locations. In this study, we used an ampicillin-digoxigenin conjugate to demonstrate by chemiluminescence that the 47-kDa lipoprotein immunogen of T. pallidum (Tpp47) is a penicillin-binding protein. Reexamination of the Tpp47 primary sequence revealed the three amino acid motifs characteristic of penicillin-binding proteins. A recombinant, nonlipidated, soluble form of Tpp47 was used to demonstrate that Tpp47 is a zinc-dependent carboxypeptidase. Escherichia coli expressing Tpp47 was characterized by cell wall abnormalities consistent with altered peptidoglycan biosynthesis. Though the inability to cultivate T. pallidum in vitro and the lack of genetic exchange systems continue to impede treponemal research, this study advances strategies for utilizing E. coli molecular genetics as a means of elucidating the complex relationships between syphilis pathogenesis and T. pallidum membrane biology.
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