ABSTRACT
An ultracentrifugally homogeneous heat-stable polysaccharide preparation free from serologically reactive rabbit testicular tissue antigen, including cardiolipin, was extracted from the Nichols strain of Treponema pallidum, and found to react by complement-fixation with homologous rabbit sera but not with human syphilitic sera. In addition, the reactive "strain-specific" component was found to be distinct from a second reactive component within the preparation related to an antigen of T. reiteri.
Subject(s)
Polysaccharides, Bacterial/isolation & purification , Treponema pallidum/immunology , Animals , Complement Fixation Tests , Humans , Immune Sera , Phospholipids , Rabbits , Species Specificity , Syphilis SerodiagnosisSubject(s)
Antibody Formation , Syphilis/immunology , Testis , Animals , Goats , Lipopolysaccharides , Lymph Nodes , Male , Phospholipids , Rabbits , Treponema/immunology , Treponema Immobilization Test , Treponema pallidum/immunologySubject(s)
Complement Fixation Tests , Syphilis Serodiagnosis , Humans , In Vitro Techniques , PhospholipidsSubject(s)
Antigens , Treponema pallidum/immunology , Animals , Bacterial Proteins , Blood , Chemical Phenomena , Chemistry , Hot Temperature , In Vitro Techniques , Lipopolysaccharides , Rabbits , UltrasonicsSubject(s)
Treponema pallidum/immunology , Antigens , Centrifugation , Lipopolysaccharides/metabolism , UltrasonicsABSTRACT
Miller, James N. (University of California School of Medicine, Los Angeles), J. H. De Bruijn, and J. H. Bekker. Immunity in experimental syphilis. IV. Serological reactivity of antigens extracted from gamma-irradiated Treponema pallidum and Treponema reiteri. J. Bacteriol. 91:583-587. 1966.-Ultrasonic lysate preparations extracted from virulent Treponema pallidum, Nichols strain, suspensions exposed to 652,800 R of gamma-irradiation exhibited a loss in the serological reactivity of their heat-labile antigens; the heat-stable components of both the lysate and residue antigens were unaffected. The activity of heat-stable, cardiolipin T. pallidum complement-fixing antigen obtained from similarly irradiated organisms was also unaltered. gamma-Irradiation of the cultivable Treponema reiteri with dosages as high as 6,500,000 R failed to alter serologically either the heat-labile or heat-stable component of its lipopolysaccharide-protein (Reiter protein) antigen. The reactivity of the lipopolysaccharide portion of the Reiter protein complex with an antiserum to T. pallidum Nichols indicates previously unsuspected antigenic differences between the rabbit-adapted Nichols strain of the organism and so-called "wild" human strains of T. pallidum in which this antigen is generally absent.
