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. 1989 Sep;57(9):2872–2877. doi: 10.1128/iai.57.9.2872-2877.1989

Major integral membrane protein immunogens of Treponema pallidum are proteolipids.

N R Chamberlain 1, M E Brandt 1, A L Erwin 1, J D Radolf 1, M V Norgard 1
PMCID: PMC313540  PMID: 2668191

Abstract

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 [DPPs]) 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.

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Selected References

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