Native surface association of a recombinant 38-kilodalton Treponema pallidum antigen isolated from the Escherichia coli outer membrane.
A recombinant plasmid designated pAW305, containing a 6-kilobase insert of Treponema pallidum DNA, directed the expression of a 38-kilodalton (kDa) treponemal antigen in Escherichia coli. The 38-kDa antigen copurified with the outer membrane fraction of the E. coli cell envelope after treatment with nonionic detergents or sucrose density gradient centrifugation. Rabbits immunized with the recombinant 38-kDa antigen developed antibodies which reacted specifically with a 38-kDa T. pallidum antigen on immunoblots, and 38-kDa antisera specifically immobilized T. pallidum in a complement-dependent manner in the T. pallidum immobilization test. Antisera to the 38-kDa recombinant antigen were also used to demonstrate its native surface association on T. pallidum by immunoelectron microscopy.
D000818:Animals; D000917:Antibody Formation; D000953:Antigens, Protozoan / Q000235:genetics* / Q000276:immunology / Q000302:isolation & purification; D000954:Antigens, Surface / Q000235:genetics / Q000276:immunology; D001425:Bacterial Outer Membrane Proteins / Q000276:immunology / Q000302:isolation & purification; D003001:Cloning, Molecular; D007114:Immunization; D008854:Microscopy, Electron; D011817:Rabbits; D011994:Recombinant Proteins / Q000276:immunology* / Q000302:isolation & purification; D014210:Treponema pallidum / Q000276:immunology* / Q000648:ultrastructure
D000953:Antigens, Protozoan; D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D011994:Recombinant Proteins