This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Stamm, L V Articles by Bassford, P J Search for Related Content PubMed PubMed Citation Articles by Stamm, L V Articles by Bassford, P J, Jr

 Previous Article  |  Next Article 

Infect Immun. 1985 March; 47(3): 799-807

Cellular and extracellular protein antigens of Treponema pallidum synthesized during in vitro incubation of freshly extracted organisms.

ABSTRACT

A new medium that permits radiolabeling of freshly extracted cells of Treponema pallidum with [35S]methionine very efficiently has been devised. Although treponemes were not purified free of contaminating rabbit tissue, label was incorporated exclusively into treponemal protein in a linear manner for at least the first 16 h of in vitro incubation. Throughout this period, virtually a full complement of treponemal proteins was synthesized, based on a sodium dodecyl sulfate-polyacrylamide gel electrophoresis comparison of the radiolabeled protein profile with the Coomassie blue-stained profile of gradient-purified treponemes. The radiolabeled protein profiles obtained with three pathogenic strains were very similar but not identical. Using solubilized treponemal extracts and a sensitive radioimmunoprecipitation procedure, we identified the protein antigens of T. pallidum that were recognized by immunoglobulin G antibodies in various rabbit and human syphilitic sera. A simple fractionation procedure has been used to separate soluble and membrane-bound treponemal proteins. A number of the membrane proteins are exposed on the cell surface, since intact radiolabeled treponemes bound antibodies directed against these proteins. In addition, a unique class of low-molecular-weight extracellular treponemal proteins has been identified. The cell surface-exposed proteins were among the earliest proteins recognized by immunoglobulin G antibodies after experimental infection of rabbits with T. pallidum.

This article has been cited by other articles:

• LaFond, R. E., Lukehart, S. A. (2006). Biological Basis for Syphilis. Clin. Microbiol. Rev. 19: 29-49 [Abstract] [Full Text]  
• Marangoni, A., Sambri, V., Storni, E., D'Antuono, A., Negosanti, M., Cevenini, R. (2000). Treponema pallidum Surface Immunofluorescence Assay for Serologic Diagnosis of Syphilis. CVI 7: 417-421 [Abstract] [Full Text]  
• Posey, J. E., Hardham, J. M., Norris, S. J., Gherardini, F. C. (1999). Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum. Proc. Natl. Acad. Sci. USA 96: 10887-10892 [Abstract] [Full Text]