Polypeptides of Treponema pallidum: Progress toward understanding their structural, functional, and immunologic roles

S. J. Norris, N. H. Axelsen, P. J. Bassford, R. E. Baughn, P. A. Hanff, P. Hindersson, R. D. Isaacs, M. A. Lovett, D. R. Blanco, S. A. Larsen, D. L. Cox, S. A. Lukehart, S. A. Baker-Zander, J. N. Miller, F. Muller, M. A. Moskophidis, G. T. Noordhoek, M. V. Norgard, C. W. Penn

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Abstract

Treponema pallidum subsp. pallidum, the spirochete that causes syphilis, is unusual in a number of respects, including its small genome size, inability to grow under standard in vitro culture conditions, microaerophilism, apparent paucity of outer membrane proteins, structurally complex periplasmic flagella, and ability to evade the host immune responses and cause disease over a period of years to decades. Many of these attributes are related ultimately to its protein content. Our knowledge of the activities, structure, and immunogenicity of its proteins has been expanded by the application of recombinant DNA, hybridoma, and structural fractionation techniques. The purpose of this monograph is to summarize and correlate this new information by using two-dimensional gel electrophoresis, monoclonal antibody reactivity, sequence data, and other properties as the bases of polypeptide identification. The protein profiles of the T. pallidum subspecies causing syphilis, yaws, and endemic syphilis are virtually indistinguishable but differ considerably from those of other treponemal species. Among the most abundant polypeptides are a group of lipoproteins of unknown function that appear to be important in the immune response during syphilitic infection. The periplasmic flagella of T. pallidum and other spirochetes are unique with regard to their protein content and ultrastructure, as well as their periplasmic location. They are composed of three core proteins (homologous to the other members of the eubacterial flagellin family) and a single, unrelated sheath protein; the functional significance of this arrangement is not understood at present. Although the bacterium contains the chaperonins GroEL and DnaK, these proteins are not under the control of the heat shock regulon as they are in most organisms. Studies of the immunogenicity of T. pallidum proteins indicate that many be useful for immunodiagnosis and immunoprotection. Future goals in T. pallidum polypeptide research include continued elucidation of their structural locations and functional activities, identification and characterization of the low-abundance outer membrane proteins, further study of the immunoprotective and immunodiagnostic potential of T. pallidum proteins, and clarification of the roles of treponemal proteins in pathogenesis.

Original languageEnglish (US)
Pages (from-to)750-779
Number of pages30
JournalMicrobiological Reviews
Volume57
Issue number3
StatePublished - Jan 1 1993

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ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology

Cite this

Norris, S. J., Axelsen, N. H., Bassford, P. J., Baughn, R. E., Hanff, P. A., Hindersson, P., Isaacs, R. D., Lovett, M. A., Blanco, D. R., Larsen, S. A., Cox, D. L., Lukehart, S. A., Baker-Zander, S. A., Miller, J. N., Muller, F., Moskophidis, M. A., Noordhoek, G. T., Norgard, M. V., & Penn, C. W. (1993). Polypeptides of Treponema pallidum: Progress toward understanding their structural, functional, and immunologic roles. Microbiological Reviews, 57(3), 750-779.