@article{mbs:/content/journal/micro/10.1099/00221287-133-6-1397, author = "Cockayne, A. and Bailey, M. J. and Penn, C. W.", title = "Analysis of Sheath and Core Structures of the Axial Filament of Treponema pallidum", journal= "Microbiology", year = "1987", volume = "133", number = "6", pages = "1397-1407", doi = "https://doi.org/10.1099/00221287-133-6-1397", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-133-6-1397", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "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.", }