Analysis of Sheath and Core Structures of the Axial Filament of Treponema Pallidum

J Gen Microbiol. 1987 Jun;133(6):1397-407. doi: 10.1099/00221287-133-6-1397.

Abstract

Electron microscopy and SDS-PAGE have been used to analyse the polypeptide and antigenic composition of the sheath and core components of the axial filament of Treponema pallidum. The sheath contains a major 37 kDa polypeptide which was solubilized by a combination of trypsin and urea treatments with concurrent loss of binding of anti-37 kDa monoclonal antibody. These studies also indicated some antigenic heterogeneity within the axial filament population. Trypsin treatment alone removed a number of antigenic determinants from the axial filament but left others intact, suggesting differences in their location within the sheath structure. A second 31.5 kDa polypeptide may also be associated with the sheath. The axial filament core comprises at least two components, an antigenically dominant 33.5 kDa polypeptide and a second of 34 kDa. The structure of the axial filament in T. pallidum and Treponema phagedenis biotype Reiterii was similar, but antigenic cross-reactivity of sheath and core components was incomplete.

MeSH terms

  • Antigens, Bacterial / analysis
  • Bacterial Proteins / analysis
  • Cross Reactions
  • Electrophoresis, Polyacrylamide Gel
  • Microscopy, Electron
  • Treponema pallidum / immunology
  • Treponema pallidum / ultrastructure*

Substances

  • Antigens, Bacterial
  • Bacterial Proteins