Analysis of sheath and core structures of the axial filament of Treponema pallidum.
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.
Cockayne
A
A
Department of Microbiology, University of Birmingham, UK.
Bailey
M J
MJ
Penn
C W
CW
D000942:Antigens, Bacterial / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D014210:Treponema pallidum / Q000276:immunology / Q000648:ultrastructure*
D000942:Antigens, Bacterial; D001426:Bacterial Proteins