Major integral membrane protein immunogens of Treponema pallidum are proteolipids

N. R. Chamberlain, M. E. Brandt, A. L. Erwin, J. D. Radolf, M. V. Norgard

Research output: Contribution to journalArticlepeer-review

80 Scopus citations


A number of the major pathogen-specific immunogens of Treponema pallidum were characterized recently as amphiphilic, integral membrane proteins by phase partitioning with Triton X-114 (J. D. Radolf, N. R. Chamberlain, A. Clausell, and M. V. Norgard. Infect. Immun. 56:490-498, 1988). In the present study, we demonstrated that the same membrane immunogens (designated as detergent phase proteins [DDPs]) become radiolabeled upon in vitro incubation of T. pallidum with various 3H-labeled fatty acids. Radioimmunoprecipitation with a monoclonal antibody confirmed that the 3H-labeled 47-kilodalton protein corresponded to the well-characterized treponemal antigen with the identical apparent molecular mass. Failure to detect 3H-labeled DPPs following incubation with erythromycin confirmed that protein acylation required de novo protein synthesis by the bacteria. When treponemes were incubated with [3H]myristate, [3H]palmitate, or [3H]oleate, radiolabeled proteins corresponding to the DPPs were detected upon autoradiography. Demonstration that a number of the abundant membrane immunogens of T. pallidum are proteolipids provides information to help clarify their membrane association(s) and may serve to explain their extraordinary immunogenicity.

Original languageEnglish (US)
Pages (from-to)2872-2877
Number of pages6
JournalInfection and immunity
Issue number9
StatePublished - 1989

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases


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