Identification of glycosylated protein antigens of Treponema pallidum and Treponema phagedenis.

Comparison of autoradiographies of intrinsically [35S] methionine and [14C] glucosamine labeled Treponema pallidum (Nichols strain) after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed four glycosylated proteins with molecular weights 30,500, 33,000, 35,000, and 59,000. T. phagedenis (biotype Reiter) was comparatively investigated and showed only two glycosylated proteins with molecular weights 33,000 and 34,000. The at the first time in treponemes identified glycosylated proteins could be precipitated with homologous human antibodies and characterized as antigens. By comparison with 125I surface labeling of T. pallidum and T. phagedenis it is suggested that the glycosylated protein antigens are localized on the surface of these treponemes.