Summary: Polypeptide and Western immunoblot profiles of subcellular fractions of ATCC 33520 have been determine by SDS-PAGE of Triton X-100-soluble and -insoluble fractions, a lipopolysaccharide-enriched fraction and purified flagella. Major Triton X-100-soluble polypeptides of 72, 68, 54 and 52 kDa were detected. The 54 kDa polypeptide appeared to be a breakdown product o a larger, heat-modifiable polypeptide. Based on the results o SDS-PAGE analysis and immunoblotting of proteinase K digests of , a ‘rough’ lipopolysaccharide appeared to be present. Electron microscopy has been used to monitor the effect of detergent treatment on the morphology o the organism and to examine the detailed structure of the flagella. Treatment with Triton removed the outer membrane, resulting in exposure of the flagella. The flagella were shown to have a complex sheath an core structure and polypeptide composition characteristic o that observed for other treponemes. Polypeptides of 38, 35, 32 and 28 kDa were present in purified flagella preparations. Immunoelectron microscopy, iodine-labelling and Western blotting were used to demonstrate the exposure o antigens on the surface. Surface iodination located polypeptides of 72, 68 and 54 kDa. Antiserum raised against whole cells of recognized these polypeptides and an additional polypeptide of 52 kDa. These data provide a basis for future detaile molecular analysis of the ultrastructure an antigenicity of .


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