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PubMed1982

Murine monoclonal antibodies specific for virulent Treponema pallidum (Nichols).

Murine anti-Treponema pallidum (Nichols) lymphocyte hybridoma cell lines secreting monoclonal antibodies against a variety of treponemal antigens have been generated. Hybridomas isolated were of three major types: those that were directed specifically against T. pallidum antigens, those that were directed against treponemal group antigens (as evidenced by their cross-reactivity with T. phagedenis biotype Reiter antigens), and those that cross-reacted with both treponemal as well as rabbit host testicular tissue antigens. The majority (31 of 39 clones) of these anti-T. pallidum hybridomas, which produced monoclonal antibodies of mouse isotypes immunoglobulin G1 (IgG1), IgG2a, IgG2b, IgG3 or IgM, were directed specifically against T. pallidum and not other treponemal or rabbit antigens tested by radioimmunoassay. Four of these T. pallidum-specific hybridomas secreted monoclonal antibodies with greater binding affinity for "aged" rather than freshly isolated intact T. pallidum cells, suggesting a possible specificity for "unmasked" surface antigens of T. pallidum. Six anti-T. pallidum hybridomas produced complement-fixing monoclonal antibodies (IgG2a, IgG2b, or IgM) that were capable of immobilizing virulent treponemes in the T. pallidum immobilization (TPI) test; these may represent biologically active monoclonal antibodies against treponemal surface antigens. Three other hybridomas secreted monoclonal antibodies which bound to both T. pallidum and T. phagedenis biotype Reiter antigens, thus demonstrating a possible specificity for treponemal group antigens. Five hybridoma cell lines were also isolated which produced IgM monoclonal antibodies that cross-reacted with all treponemal and rabbit host testicular tissue antigens employed in the radioimmunoassays. This report describes the construction and characteristics of these hybridoma cell lines. The potential applications of the anti-T. pallidum monoclonal antibodies are discussed.

Aging↗
PubMed1984

Monoclonal antibody analysis of specific antigenic similarities among pathogenic Treponema pallidum subspecies.

Murine monoclonal antibodies directed against a 47,000-dalton immunodominant surface-exposed antigen of Treponema pallidum subsp. pallidum (Nichols) were isolated. These monoclonal antibodies cross-reacted with analogous 47,000-dalton antigens of two other virulent treponemes, T. pallidum subsp. pertenue and T. pallidum subsp. endemicum (Bosnia A), as determined by radioimmunoassay and immunoblot analyses. Immunoelectron microscopy confirmed that the 47,000-dalton antigen of T. pallidum subsp. pallidum was a surface-associated cellular component. Surface binding assays and immunoelectron microscopic studies also suggested that the analogous 47,000-dalton antigenic component of T. pallidum subsp. pertenue may not have been oriented toward the bacterial surface in the same way as the T. pallidum subsp. pallidum antigen or that the relevant antigenic determinant(s) may not have been exposed to the outer surface in the same way. The significance of this antigen relative to its apparent conservation among pathogenic treponemes and its possible diagnostic and vaccinogenic potentials are discussed.

Animals↗
PubMed1986

Molecular specificities of monoclonal antibodies directed against virulent Treponema pallidum.

Radioimmunoprecipitation (RIP) and Western blot analyses with specific anti-Treponema pallidum subsp. pallidum monoclonal antibodies were used to identify antigens with apparent masses of 102, 84, 54, 53, 52, 47, 32, 29, and 24 kilodaltons (kDa). Cross-reactivity of these antibodies with T. pallidum subsp. pertenue antigens and lack of cross-reactivity with T. phagedenis biotype Reiter, T. vincentii, T. refringens, T. scoliodontum, and T. denticola were also demonstrated by RIP and Western blot analyses. Reactivities in the T. pallidum immobilization test, along with the RIP of lactoperoxidase-catalyzed iodination products, suggested that the identified antigens were surface associated. The abundance and surface association of the 47- and 84-kDa antigens were supported by reactivity in the microhemagglutination test for T. pallidum and by strong reactivity of monoclonal antibodies upon indirect immunofluorescence assays with rabbit-cultivated T. pallidum subsp. pallidum, respectively, but not with T. phagedenis biotype Reiter. Anti-47-kDa and anti-84-kDa monoclonal antibodies were also reactive in indirect immunofluorescence assays using treponemes found in dark-field-positive smears of human genital ulcers.

Animals↗
PubMed1989

Treponema pallidum-immobilizing antibodies in guinea pig experimental syphilis.

Treponema pallidum-immobilizing (TPI) antibodies were examined in intradermally infected inbred strain 13 and adoptively immune inbred strain 2 guinea pigs. Both strains of animals produced TPI antibodies at or after 90 days of infection. TPI antibodies were not associated with the protective mechanism(s) operative after challenge in adoptively immune animals.

Animals↗
PubMed1972

Shape of Treponema pallidum.

Treponema pallidum was found to be not helical, but a flat wave twisted into one to five different planes per cell.

Bacteriological Techniques↗
PubMed1985

Humoral response of the mouse to Treponema pallidum.

To investigate the development of the humoral immune response of mice to infection with Treponema pallidum, Balb/c and C57Bl mice were injected intradermally with 10 x 10(6) virulent organisms. Serum samples were taken from the mice at weekly intervals after infection and used in the electrophoretic transblotting technique to detect T pallidum and T phagedenis biotype Reiter antigens. The serum samples taken from infected mice at 21, 42, 84, and 126 days after infection recognised two to 15 T pallidum antigens, with a gradual but continual increase in the number of antigens recognised. The same antisera to T pallidum recognised five cross reactive T phagedenis biotype Reiter antigens. Mice injected with 10 x 10(6) heat killed T pallidum organisms failed to recognise T pallidum antigens, as shown by the blotting technique. When mice infected with T pallidum were given antibiotics, the development of the humoral response was interrupted. These experiments indicated that mice respond more slowly than rabbits to T pallidum, which may be because T pallidum is weakly immunogenic in mice.

Animals↗
PubMed1986

Antigenic contents of Treponema pallidum preparations.

In investigations of syphilis various Treponema pallidum antigens are used to study the immune responses of naturally or experimentally infected hosts. In the past these antigen preparations have rarely been examined for their antigenic contents and activity. In the present study, supernatant, sediment, and solubilised preparations of T pallidum Nichols strain (20 X 10(9) organisms/ml) and T phagedenis biotype Reiter were examined by modified counterimmunoelectrophoresis and immunoblotting for their antigenic contents. No T pallidum antigen was seen in the supernatant fraction, which contained cross reacting (Reiter) antigens and rabbit serum proteins. The remaining T pallidum preparations contained T pallidum antigens, cross reacting treponemal (Reiter) antigens, and rabbit serum proteins. These findings suggest that T pallidum preparations should be examined qualitatively and quantitatively before they are used for monitoring immune responses and interpreting data. Technology for these examinations is available.

Animals↗
PubMed1990

Rapid in vitro immobilisation of purified Treponema pallidum (Nichols strain), and protection by extraction fluids from rabbit testes.

The use of Percoll-purified treponemes in an assay similar to the Treponema pallidum Immobilisation test demonstrated that immobilisation of purified treponemes by seronegative normal human serum proceeded at a much higher rate than that of unpurified treponemes. This suggests that the removal of the testicular extract makes the treponemes more vulnerable to this action. A preincubation of the purified treponemes with the testicular extract from infected or uninfected testes delayed their rate of immobilisation to that demonstrated by the unpurified treponemes. This showed that substances produced during the infection are probably not responsible for the delay in immobilisation. Discrimination between the classical and the alternative pathway of complement activation, studied by the ethylene glycol-bis (beta-aminoethyl ether) N,N,N',N'-tetraacetic acid (EGTA) method, showed that the classical pathway was responsible for the rapid immobilisation of the purified treponemes. However, the slow immobilisation in the EGTA-serum samples suggested a minor role of the alternative pathway in the immobilisation of the purified treponemes. Since the testicular extracts exerted an anti-complement activity, it needs to be investigated whether the protection offered to the purified treponemes by the testicular extracts is based on their deteriorating effect on the classical complement pathway or is due to a re-establishment of the protective cover around the treponemes.

Animals↗
PubMed1985

Immune immobilization of Treponema pallidum: antibody and complement interactions revisited.

The Treponema pallidum immobilization test was designed for serodiagnosis of syphilis and is dependent upon specific antibody and a heat labile component of normal serum. Investigators have shown the component to be dependent upon divalent cations and it is presumed to be complement. Experiments were performed to reevaluate the interactions of antibody and complement and the mechanism of immobilization. The loss of treponemal motility was correlated to the loss of complement activity in the reaction mixture. When motility of treponemes incubated with immune serum IgG and complement had dropped to 50% (3.4 h), 72% of the available complement had been consumed. At the same time, treponemes incubated with normal serum IgG and complement were 82% motile and only 51% of the complement had been consumed. C6 deficient rabbit serum and C4 deficient guinea pig serum were used in conjunction with immune serum IgG to determine which components of the complement cascade were necessary for immobilization. Treponemes were not immobilized by either sera. Results suggest that the heat labile factor in normal sera is complement, that both early and late components of the complement cascade are necessary, and that the reaction proceeds via the classical complement pathway. Although T. pallidum is susceptible to the actions of antibody and complement, the organisms must interact with these components for at least 2 h before immobilization will result.

Animals↗
PubMed1985

Immobilization and neutralization of Treponema pallidum attached to cultured mammalian cells.

The in vitro effects of antibodies, complement, and (or) macrophages on Treponema pallidum have been previously characterized using relatively simple systems of organisms incubated with the immune components. In vivo, the more complex environment may alter immune reactivity. Experiments were performed to determine whether immobilizing and neutralizing antibodies retained their effectiveness in a more complex environment involving cultured mammalian cells. Two different protocols were used. In protocol A treponemes and normal or immune serum were mixed and added immediately to the cultured cells. In protocol B treponemes were preincubated for 18 h with cultured cells to maximize treponemal attachment; then normal or immune serum was added. With both protocols, attachment of organisms resulted in less efficient immobilization and neutralization. In further experiments, cultured cells were disrupted with Triton X, leaving cytoskeletal remnants on the vessel surface. Identical immobilization and neutralization experiments were performed in the presence of these remnants. In contrast to the findings with viable cultured cells, treponemal attachment to these nonviable remnants did not effect either antibody reaction. Attached organisms were immobilized or neutralized just as efficiently as unattached organisms. Results are discussed in terms of the altered immune reactivity in more complex in vitro environments.

Animals↗
PubMed1986

Extensive cross reactivity between Treponema pallidum and cultivable treponemes demonstrated by sequential immunoadsorption.

Extensive cross reactivity between Treponema pallidum and three nonpathogenic species of treponemes was demonstrated by the Western blot technique. Rabbit antiserum produced by adjuvant immunization with solubilized T. pallidum antigens reacted with 34 T. pallidum antigens and with approximately 30 antigens each of T. phagedenis biotype Reiter, T. noguchii and T. vincentii. Adsorption of the antiserum with T. phagedenis Reiter removed only about half of the cross-reacting antibodies. Sequential adsorption with all three nonpathogenic treponemes removed antibodies to all but three polypeptides of 36,000, 34,000 and 27,000 daltons.

Animals↗
PubMed1999

Immunization with Treponema pallidum outer membrane vesicles induces high-titer complement-dependent treponemicidal activity and aggregation of T. pallidum rare outer membrane proteins (TROMPs).

The purpose of this study was to determine whether immunization with purified outer membrane vesicles (OMV) from Treponema pallidum (T.p. ) could elicit Abs capable of killing this organism. It is well established that the immunization of rabbits or mice with killed T.p. or with recombinant T.p. Ags has failed to generate serum killing activity comparable with that of infection-derived immunity. Because of the small amount of T.p. OMV obtainable, a single mouse was immunized with purified OMV. The mouse anti-OMV serum and infection-derived immune rabbit serum (IRS) were compared by reactivities on two-dimensional T.p. immunoblots and by the T.p. immobilization test, a complement-dependent killing assay. Whereas IRS detected >40 Ags, the anti-OMV serum identified only 6 Ags corresponding to proteins identified previously in the outer membrane. T.p. immobilization testing showed that IRS had a 100% killing titer of 1:44 and a 50% killing titer of 1:662. By comparison, the mouse anti-OMV serum had a significantly greater 100% killing titer of 1:1,408 and a 50% killing titer of 1:16,896. Absorption of the anti-OMV serum to remove Ab against outer membrane-associated lipoproteins did not change the 100% killing titer. Freeze-fracture analysis of T.p. incubated in IRS or anti-OMV serum showed that T.p. rare membrane-spanning outer membrane proteins were aggregated. This is the first demonstration of high-titer killing Abs resulting from immunization with defined T.p. molecules; our study indicates that the targets for these Abs are T. p. rare outer membrane proteins.

Animals↗
PubMed1956

The Treponema pallidum immobilization test.

The authors first discuss the principle of the Treponema pallidum immobilization (TPI) test, considered both as a qualitative and as a quantitative test, and then various specific aspects of passage of the Nichols strain of treponeme in rabbit testes. A number of important technical details and modifications in the test procedure are then reviewed, and the clinical value of the test is discussed.The sensitivity of the TPI test is considerably greater than that of the serological tests for syphilis more usually performed, and its specificity is also remarkably high. However, it is stressed that, at the present stage of development, the greatest value of the TPI test lies in its use as an excellent aid to diagnosis rather than as a test of cure.

Animals↗
PubMed1987

Humoral response in Treponema pallidum-infected guinea pigs: I. Antibody specificity.

Young male inbred strain 2 guinea pigs were infected intradermally with 8 X 10(7) Treponema pallidum extracted from a rabbit orchitis, and 5 months later reinfected with 10(7) T. pallidum. Ninety percent of the animals developed symptomatic lesions after initial infection but none on challenge. Immunoblotting of sera obtained at intervals after infection or reinfection showed antibodies against T. pallidum antigen (TP), nonpathogenic treponemes--T. phagedenis biotype Reiter (TR), T. refringens strain Noguchi (TN), and T. vincentii (TV)--as well as normal rabbit serum (NRS) and normal rabbit testes extract (NRT). Antibodies reacting with TP were detected as early as 17 days (five polypeptides) and steadily rose (at 3 months 17 polypeptides were seen). Cross-reacting antibodies to TR, TN, TV, or rabbit proteins decreased within 3 to 5 months. After reinfection, the antibodies to NRS increased more sharply than the anti-treponemal antibodies. Adsorption with TR and NRS of sera obtained after infection or reinfection produced a reduction of antibodies to TP by 75-87%.

Animals↗
PubMed1979

Electron microscopy of treponemes subjected to the Treponema pallidum immobilization (TPI) test. II. Immunoelectron microscopy.

The experiments were carried out in order to investigate whether human IgG globulin is absorbed on to the surface of T. pallidum cells during incubation with human syphilis serum in the Treponema pallidum immobilization (TPI) test. Cells of T. pallidum Nichols subjected to the TPI test were further incubated with ferritin conjugated rabbit antihuman IgG globulin. Human IgG globulin could only be demonstrated on immunoimmobilized cells, i.e. cells incubated with human syphilis serum and unheated guinea pig serum (GPS). The surface of the swollen cells was completely covered by a fuzzy layer on to which the ferritin molecules appeared to be attached. In ultrathin sections of cells obtained from the same suspensions the surface of the outer cell membrane was outlined by ferritin molecules. In these cells a rather wide gap was observed between the outer membrane and the cytoplasmic membrane. The ribosomes seemed to have disappeared from the cytoplasm of the immunoimmobilized treponemes, but were present in motile cells obtained from control incubations.

Adsorption↗
PubMed1985

Characterization of monoclonal antibodies to Treponema pallidum.

Thirteen hybrid cell lines which produce mouse monoclonal antibodies to Treponema pallidum, the causative agent of syphilis, have been established. All of the monoclonal antibodies react with T. pallidum, Nichols strain, in ELISA and in immunofluorescence assays, but do not react with normal rabbit testicular tissue in the ELISA. Two of these antibodies were demonstrated to react with the nonpathogenic treponemes T. phagedenis, biotype Reiter, T. refringens (Noguchi strain), T. vincentii, and T. denticola (strains 11 and W), as well as with Borrelia recurrentis, Leptospira interrogans, serogroup Canicola, and the swine pathogen T. hyodysenteriae. The remaining 11 antibodies react with four recently isolated strains of T. pallidum, but with none of the related nonpathogens nor with Borrelia or Leptospira. Thus, our results to date indicate that these monoclonal antibodies may identify antigenic determinants that are specific either for T. pallidum alone or for those treponemes which are pathogenic for humans. The molecular specificities of six of the 13 antibodies were determined by Western blotting. We anticipate potential usefulness of these antibodies in the investigation of the antigenic structure of T. pallidum, the taxonomic study of the pathogenic and nonpathogenic treponemes, and in the diagnosis of syphilis.

Animals↗
PubMed1982

Identification of Treponema pallidum antigens: comparison with a nonpathogenic treponeme.

The major antigens of Treponema pallidum, Nichols strain were examined by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting techniques. Organisms were extracted from rabbit testes, purified by differential centrifugation, washed, and disrupted by sonication before solubilization in SDS buffer, SDS-PAGE analysis on 12.5% gels revealed at least 35 distinguishable polypeptides with molecular weights between 14,000 and 100,000. Proteins were electrophoretically transferred from gels to nitrocellulose paper and were stained with pooled rabbit anti-T. pallidum serum (IRS) and 125I-protein A. At least eight distinct antigenic molecules were revealed, with the major component residing at 48,000 daltons. Extensive washing of T. pallidum before solubilization did not alter the antigenic profile. Five molecules with common treponemal antigenic determinants were identified both by staining blots of T. phagedenis, biotype Reiter with IRS and by staining blots of T. pallidum with rabbit anti-Reiter antiserum. Three putative T. pallidum-specific antigens were identified by staining T. pallidum with IRS that had been extensively adsorbed with Reiter treponemes.

Animals↗
PubMedDate not supplied

The humoral immune response in rabbits infected with Treponema pallidum: Comparison of antibody levels measured by the staphylococcal protein A-IgG (SPA-TP) microassay with VDRL, FTA-Abs, and TPI antibody responses during the development of acquired resistance to challenge.

The ontogeny of the immunoglobulin G (IgG) immune response in experimental syphilis was determined by use of an antitreponemal microassay (SPA-TP) in which radioiodinated staphylococcal protein A (SPA) was used. Results were compared with those obtained in the same rabbits by use of the Venereal Disease Research Laboratory (VDRL), fluorescent treponemal antibody-absorption (FTA-Abs), and Treponema pallidium immobilization (TPI) tests. Of the four serologic tests, only the SPA-TP and TPI assays gave results that correlated significantly over the entire 17-month period of infection. Preliminary evidence indicated that the antibody detected by the SPA-TP microassay may correlate quantitatively with the state of host immunity as determined by in vivo challenge; if this finding is confirmed, the SPA-TP microassay could be applied for assessment of the immune status in syphilis.

Animals↗