This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Akins, D. R.
Right arrow Articles by Radolf, J. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Akins, D. R.
Right arrow Articles by Radolf, J. D.

 Previous Article  |  Next Article 

J. Bacteriol., Aug 1997, 5076-5086, Vol 179, No. 16
Copyright © 1997, American Society for Microbiology

Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membrane

DR Akins, E Robinson, D Shevchenko, C Elkins, DL Cox and JD Radolf
Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235, USA.

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.


This article has been cited by other articles:

  • Deka, R. K., Brautigam, C. A., Tomson, F. L., Lumpkins, S. B., Tomchick, D. R., Machius, M., Norgard, M. V. (2007). Crystal Structure of the Tp34 (TP0971) Lipoprotein of Treponema pallidum: IMPLICATIONS OF ITS METAL-BOUND STATE AND AFFINITY FOR HUMAN LACTOFERRIN. J. Biol. Chem. 282: 5944-5958 [Abstract] [Full Text]  
  • Hazlett, K. R. O., Cox, D. L., Decaffmeyer, M., Bennett, M. P., Desrosiers, D. C., La Vake, C. J., La Vake, M. E., Bourell, K. W., Robinson, E. J., Brasseur, R., Radolf, J. D. (2005). TP0453, a Concealed Outer Membrane Protein of Treponema pallidum, Enhances Membrane Permeability. J. Bacteriol. 187: 6499-6508 [Abstract] [Full Text]  
  • Champion, C. I., Blanco, D. R., Lovett, M. A. (2005). Quantitative Assessment of Protection in Experimental Syphilis. Infect. Immun. 73: 5923-5927 [Abstract] [Full Text]  
  • Nikaido, H. (2003). Molecular Basis of Bacterial Outer Membrane Permeability Revisited. Microbiol. Mol. Biol. Rev. 67: 593-656 [Abstract] [Full Text]  
  • Hazlett, K. R. O., Rusnak, F., Kehres, D. G., Bearden, S. W., La Vake, C. J., La Vake, M. E., Maguire, M. E., Perry, R. D., Radolf, J. D. (2003). The Treponema pallidum tro Operon Encodes a Multiple Metal Transporter, a Zinc-dependent Transcriptional Repressor, and a Semi-autonomously Expressed Phosphoglycerate Mutase. J. Biol. Chem. 278: 20687-20694 [Abstract] [Full Text]  
  • Lee, Y.-H., Dorwart, M. R., Hazlett, K. R. O., Deka, R. K., Norgard, M. V., Radolf, J. D., Hasemann, C. A. (2002). The Crystal Structure of Zn(II)-Free Treponema pallidum TroA, a Periplasmic Metal-Binding Protein, Reveals a Closed Conformation. J. Bacteriol. 184: 2300-2304 [Abstract] [Full Text]  
  • Hazlett, K. R.O., Sellati, T. J., Nguyen, T. T., Cox, D. L., Clawson, M. L., Caimano, M. J., Radolf, J. D. (2001). The Tprk Protein of Treponema pallidum Is Periplasmic and Is Not a Target of Opsonic Antibody or Protective Immunity. JEM 193: 1015-1026 [Abstract] [Full Text]  
  • Centurion-Lara, A., Godornes, C., Castro, C., Van Voorhis, W. C., Lukehart, S. A. (2000). The tprK Gene Is Heterogeneous among Treponema pallidum Strains and Has Multiple Alleles. Infect. Immun. 68: 824-831 [Abstract] [Full Text]  
  • Zhang, H. H., Blanco, D. R., Exner, M. M., Shang, E. S., Champion, C. I., Phillips, M. L., Miller, J. N., Lovett, M. A. (1999). Renaturation of Recombinant Treponema pallidum Rare Outer Membrane Protein 1 into a Trimeric, Hydrophobic, and Porin-Active Conformation. J. Bacteriol. 181: 7168-7175 [Abstract] [Full Text]  
  • Arroll, T. W., Centurion-Lara, A., Lukehart, S. A., Van Voorhis, W. C. (1999). T-Cell Responses to Treponema pallidum subsp. pallidum Antigens during the Course of Experimental Syphilis Infection. Infect. Immun. 67: 4757-4763 [Abstract] [Full Text]  
  • Blanco, D. R., Whitelegge, J. P., Miller, J. N., Lovett, M. A. (1999). Demonstration by Mass Spectrometry that Purified Native Treponema pallidum Rare Outer Membrane Protein 1 (Tromp1) Has a Cleaved Signal Peptide. J. Bacteriol. 181: 5094-5098 [Abstract] [Full Text]  
  • Centurion-Lara, A., Castro, C., Barrett, L., Cameron, C., Mostowfi, M., Van Voorhis, W. C., Lukehart, S. A. (1999). Treponema pallidum Major Sheath Protein Homologue Tpr K Is a Target of Opsonic Antibody and the Protective Immune Response. JEM 189: 647-656 [Abstract] [Full Text]  
  • Cameron, C. E., Castro, C., Lukehart, S. A., Van Voorhis, W. C. (1998). Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase. Infect. Immun. 66: 5763-5770 [Abstract] [Full Text]  
  • Fraser, C. M., Norris, S. J., Weinstock, G. M., White, O., Sutton, G. G., Dodson, R., Gwinn, M., Hickey, E. K., Clayton, R., Ketchum, K. A., Sodergren, E., Hardham, J. M., McLeod, M. P., Salzberg, S., Peterson, J., Khalak, H., Richardson, D., Howell, J. K., Chidambaram, M., Utterback, T., McDonald, L., Artiach, P., Bowman, C., Cotton, M. D., Fujii, C., Garland, S., Hatch, B., Horst, K., Roberts, K., Sandusky, M., Weidman, J., Smith, H. O., Venter, J. C. (1998). Complete Genome Sequence of Treponema pallidum, the Syphilis Spirochete. Science 281: 375-388 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»