THE AXIAL FILAMENT ANTIGEN OF TREPONEMA-PALLIDUM

  • 1 January 1985
    • journal article
    • research article
    • Vol. 54  (4) , 635-641
Abstract
Axial filaments (flagella) of T. pallidum were purified in large enough quantities to be analyzed electrophoretically. They produced a characteristic linear precipitate in 2-dimensional immunoelectrophoresis. Polyacrylamide gel electrophoresis showed 3 major polypeptides, the most prominent having an apparent MW of 37,000, .apprx. 1500 less than the corresponding component of axial filaments of the Reiter trepneme. A doublet of less abundant polypeptides of 33,500-34,000 MW also differed slightly from those of the Reiter treponeme. Western blot analysis showed that the principal polypeptide of the T. pallidum axial filament was strongly antigenic, and antibody to it was prominent in sera from hyperimmunized, as well as acutely infected (orchitic), rabbits, and in soluble fractions from acutely infected rabbit testes from which large numbers of viable treponemes had been extracted. This indicated that antibody to this component was ineffective treponemes from the tissue.

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