Isolation and characterization of antigens from Treponema phagedenis biotype Reiter cross-reacting with Treponema pallidum.

The specific aims of the studies reviewed here were to design a rational purification strategy for Reiter treponeme antigens using combinations of different chromatographic principles, to isolate and characterize the Reiter treponemal antigens, especially the antigens labelled TR-b, TR-c, TR-dl, TR-d2, and TR-e cross-reacting with antigens in Treponema pallidum, to develop and evaluate the use of these purified antigens in syphilis diagnostic enzyme-linked immunosorbent assays (ELISA), to investigate whether Reiter treponeme antigens can induce protective immunity against experimental syphilis in rabbits. By combining anion exchange chromatography, gel filtration, agarose gel electrophoresis, hydrophobic interaction chromatography, and affinity chromatography on Iminodiacetic acid-Sepharose CL 4B and Lysine Sepharose 4B we were able to isolate seven different water soluble Reiter antigens from one single Reiter sonicate supernatant (I, II, III, IV, V, VI). The applied chromatographic matrices were selected due to their efficiency for separation of the Reiter antigens in pilot experiments. In addition to the above mentioned Reiter antigens additional antigens labelled TR-o (V) and LPS (VI) were isolated. TR-b, TR-c, and TR-o were shown to be protein antigens (III, IV, V). The TR-c antigen of the Reiter treponeme cross-reacted not only with an antigen in T. pallidum but also with an antigen common to a wide range of bacteria (IX). The TR-d antigen composed of a ribonucleic acid component (TR-dl) (II) and a protein component (TR-d2). The TR-e antigen represented the flagellum of the bacterium (I), and the LPS antigen was a pure lipopolysaccharide antigen (VI).(ABSTRACT TRUNCATED AT 250 WORDS)