%0 Journal Article %A Cockayne, A. %A Bailey, M. J. %A Penn, C. W. %T Analysis of Sheath and Core Structures of the Axial Filament of Treponema pallidum %D 1987 %J Microbiology, %V 133 %N 6 %P 1397-1407 %@ 1465-2080 %R https://doi.org/10.1099/00221287-133-6-1397 %I Microbiology Society, %X Summary: 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. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-133-6-1397