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Journal of Clinical Microbiology logoLink to Journal of Clinical Microbiology
. 1990 Jul;28(7):1600–1607. doi: 10.1128/jcm.28.7.1600-1607.1990

A new attempt to distinguish serologically the subspecies of Treponema pallidum causing syphilis and yaws.

G T Noordhoek 1, A Cockayne 1, L M Schouls 1, R H Meloen 1, E Stolz 1, J D van Embden 1
PMCID: PMC267996  PMID: 2199521

Abstract

In an effort to serologically differentiate syphilis from yaws, 69 monoclonal antibody species raised against Treponema pallidum subsp. pallidum were tested by immunoblotting for their reactivity with Treponema pallidum subsp. pertenue. All monoclonal antibodies reacted with antigens with the same molecular weight of both subspecies. Furthermore, no differences in reactivity between sera from yaws patients and from syphilis patients were found by Western blot (immunoblot) analysis of cell lysates of T. pallidum subsp. pallidum and T. pallidum subsp. pertenue. We tried to exploit the only known molecular difference between the subspecies. The subunits of the 190-kilodalton multimeric proteins TpF1 and TyF1 of T. pallidum subsp. pallidum and T. pallidum subsp. pertenue, respectively, have previously been shown to differ in one amino acid residue at position 40. In this study, no difference was found in immunoreactivity of TpF1 or TyF1 with either syphilis sera or yaws sera. Synthetic peptides based on the sequence of TpF1 and of TyF1 were used in an enzyme-linked immunosorbent assay with syphilis sera and yaws sera. Again, no difference in reactivity between the T. pallidum subsp. pallidum- and T. pallidum subsp. pertenue-derived peptides was observed.

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Selected References

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  1. Alderete J. F., Baseman J. B. Analysis of serum IgG against Treponema pallidum protein antigens in experimentally infected rabbits. Br J Vener Dis. 1981 Oct;57(5):302–308. doi: 10.1136/sti.57.5.302. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bailey M. J., Cockayne A., Penn C. W. Monoclonal antibodies directed against surface-associated polypeptides of Treponema pallidum define a biologically active antigen. J Gen Microbiol. 1987 Jul;133(7):1793–1803. doi: 10.1099/00221287-133-7-1793. [DOI] [PubMed] [Google Scholar]
  3. Bailey M. J., Cockayne A., Penn C. W. Production of murine monoclonal antibodies to the major axial filament polypeptide of Treponema pallidum. J Gen Microbiol. 1987 Jul;133(7):1805–1813. doi: 10.1099/00221287-133-7-1805. [DOI] [PubMed] [Google Scholar]
  4. Bailey M. J., Thomas C. M., Cockayne A., Strugnell R. A., Penn C. W. Cloning and expression of Treponema pallidum antigens in Escherichia coli. J Gen Microbiol. 1989 Sep;135(9):2365–2378. doi: 10.1099/00221287-135-9-2365. [DOI] [PubMed] [Google Scholar]
  5. Baker-Zander S. A., Hook E. W., 3rd, Bonin P., Handsfield H. H., Lukehart S. A. Antigens of Treponema pallidum recognized by IgG and IgM antibodies during syphilis in humans. J Infect Dis. 1985 Feb;151(2):264–272. doi: 10.1093/infdis/151.2.264. [DOI] [PubMed] [Google Scholar]
  6. Baker-Zander S. A., Lukehart S. A. Molecular basis of immunological cross-reactivity between Treponema pallidum and Treponema pertenue. Infect Immun. 1983 Nov;42(2):634–638. doi: 10.1128/iai.42.2.634-638.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Baseman J. B., Hayes E. C. Molecular characterization of receptor binding proteins and immunogens of virulent Treponema pallidum. J Exp Med. 1980 Mar 1;151(3):573–586. doi: 10.1084/jem.151.3.573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Baughn R. E., Adams C. B., Musher D. M. Circulating immune complexes in experimental syphilis: identification of treponemal antigens and specific antibodies to treponemal antigens in isolated complexes. Infect Immun. 1983 Nov;42(2):585–593. doi: 10.1128/iai.42.2.585-593.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Fehniger T. E., Radolf J. D., Lovett M. A. Properties of an ordered ring structure formed by recombinant Treponema pallidum surface antigen 4D. J Bacteriol. 1986 Mar;165(3):732–739. doi: 10.1128/jb.165.3.732-739.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fehniger T. E., Walfield A. M., Cunningham T. M., Radolf J. D., Miller J. N., Lovett M. A. Purification and characterization of a cloned protease-resistant Treponema pallidum-specific antigen. Infect Immun. 1984 Nov;46(2):598–607. doi: 10.1128/iai.46.2.598-607.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fohn M. J., Wignall S., Baker-Zander S. A., Lukehart S. A. Specificity of antibodies from patients with pinta for antigens of Treponema pallidum subspecies pallidum. J Infect Dis. 1988 Jan;157(1):32–37. doi: 10.1093/infdis/157.1.32. [DOI] [PubMed] [Google Scholar]
  12. Garner M. F., Backhouse J. L., Daskalopoulos G., Walsh J. L. Treponema pallidum haemagglutination test for yaws. Comparison with the TPI and FTA-ABS tests. Br J Vener Dis. 1972 Dec;48(6):479–482. doi: 10.1136/sti.48.6.479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Geysen H. M., Barteling S. J., Meloen R. H. Small peptides induce antibodies with a sequence and structural requirement for binding antigen comparable to antibodies raised against the native protein. Proc Natl Acad Sci U S A. 1985 Jan;82(1):178–182. doi: 10.1073/pnas.82.1.178. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Geysen H. M., Meloen R. H., Barteling S. J. Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proc Natl Acad Sci U S A. 1984 Jul;81(13):3998–4002. doi: 10.1073/pnas.81.13.3998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hanff P. A., Bishop N. H., Miller J. N., Lovett M. A. Humoral immune response in experimental syphilis to polypeptides of Treponema pallidum. J Immunol. 1983 Oct;131(4):1973–1977. [PubMed] [Google Scholar]
  16. Hanff P. A., Fehniger T. E., Miller J. N., Lovett M. A. Humoral immune response in human syphilis to polypeptides of Treponema pallidum. J Immunol. 1982 Sep;129(3):1287–1291. [PubMed] [Google Scholar]
  17. Hansen E. B., Pedersen P. E., Schouls L. M., Severin E., van Embden J. D. Genetic characterization and partial sequence determination of a Treponema pallidum operon expressing two immunogenic membrane proteins in Escherichia coli. J Bacteriol. 1985 Jun;162(3):1227–1237. doi: 10.1128/jb.162.3.1227-1237.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Hensel U., Wellensiek H. J., Bhakdi S. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis immunoblotting as a serological tool in the diagnosis of syphilitic infections. J Clin Microbiol. 1985 Jan;21(1):82–87. doi: 10.1128/jcm.21.1.82-87.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Hook E. W., 3rd, Roddy R. E., Lukehart S. A., Hom J., Holmes K. K., Tam M. R. Detection of Treponema pallidum in lesion exudate with a pathogen-specific monoclonal antibody. J Clin Microbiol. 1985 Aug;22(2):241–244. doi: 10.1128/jcm.22.2.241-244.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Ijsselmuiden O. E., Meinardi M. M., van der Sluis J. J., Menke H. E., Stolz E., van Eijk R. V. Enzyme-linked immunofiltration assay for rapid serodiagnosis of syphilis. Eur J Clin Microbiol. 1987 Jun;6(3):281–285. doi: 10.1007/BF02017613. [DOI] [PubMed] [Google Scholar]
  21. Jones S. A., Marchitto K. S., Miller J. N., Norgard M. V. Monoclonal antibody with hemagglutination, immobilization, and neutralization activities defines an immunodominant, 47,000 mol wt, surface-exposed immunogen of Treponema pallidum (Nichols). J Exp Med. 1984 Nov 1;160(5):1404–1420. doi: 10.1084/jem.160.5.1404. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Lukehart S. A., Baker-Zander S. A., Gubish E. R., Jr Identification of Treponema pallidum antigens: comparison with a nonpathogenic treponeme. J Immunol. 1982 Aug;129(2):833–838. [PubMed] [Google Scholar]
  23. Marchitto K. S., Jones S. A., Schell R. F., Holmans P. L., Norgard M. V. Monoclonal antibody analysis of specific antigenic similarities among pathogenic Treponema pallidum subspecies. Infect Immun. 1984 Sep;45(3):660–666. doi: 10.1128/iai.45.3.660-666.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Menke H. E., Veldkamp J., Brunings E. A., Niemel P. L., Notowicz A., Stolz E. Comparison of cardiolipin and treponemal tests in the serodiagnosis of yaws. Br J Vener Dis. 1979 Apr;55(2):102–104. doi: 10.1136/sti.55.2.102. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Moskophidis M., Müller F. Molecular analysis of immunoglobulins M and G immune response to protein antigens of Treponema pallidum in human syphilis. Infect Immun. 1984 Jan;43(1):127–132. doi: 10.1128/iai.43.1.127-132.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Moskophidis M., Müller F. Monoclonal antibodies to immunodominant surface-exposed protein antigens of Treponema pallidum. Eur J Clin Microbiol. 1985 Oct;4(5):473–477. doi: 10.1007/BF02014427. [DOI] [PubMed] [Google Scholar]
  27. Noordhoek G. T., Hermans P. W., Paul A. N., Schouls L. M., van der Sluis J. J., van Embden J. D. Treponema pallidum subspecies pallidum (Nichols) and Treponema pallidum subspecies pertenue (CDC 2575) differ in at least one nucleotide: comparison of two homologous antigens. Microb Pathog. 1989 Jan;6(1):29–42. doi: 10.1016/0882-4010(89)90005-3. [DOI] [PubMed] [Google Scholar]
  28. Noordhoek G. T., Wieles B., van der Sluis J. J., van Embden J. D. Polymerase chain reaction and synthetic DNA probes: a means of distinguishing the causative agents of syphilis and yaws? Infect Immun. 1990 Jun;58(6):2011–2013. doi: 10.1128/iai.58.6.2011-2013.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Norgard M. V., Selland C. K., Kettman J. R., Miller J. N. Sensitivity and specificity of monoclonal antibodies directed against antigenic determinants of Treponema pallidum Nichols in the diagnosis of syphilis. J Clin Microbiol. 1984 Oct;20(4):711–717. doi: 10.1128/jcm.20.4.711-717.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Norris S. J., Sell S. Antigenic complexity of Treponema pallidum: antigenicity and surface localization of major polypeptides. J Immunol. 1984 Nov;133(5):2686–2692. [PubMed] [Google Scholar]
  31. Radolf J. D., Lernhardt E. B., Fehniger T. E., Lovett M. A. Serodiagnosis of syphilis by enzyme-linked immunosorbent assay with purified recombinant Treponema pallidum antigen 4D. J Infect Dis. 1986 Jun;153(6):1023–1027. doi: 10.1093/infdis/153.6.1023. [DOI] [PubMed] [Google Scholar]
  32. Robertson S. M., Kettman J. R., Miller J. N., Norgard M. V. Murine monoclonal antibodies specific for virulent Treponema pallidum (Nichols). Infect Immun. 1982 Jun;36(3):1076–1085. doi: 10.1128/iai.36.3.1076-1085.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Schouls L. M., Ijsselmuiden O. E., Weel J., van Embden J. D. Overproduction and purification of Treponema pallidum recombinant-DNA-derived proteins TmpA and TmpB and their potential use in serodiagnosis of syphilis. Infect Immun. 1989 Sep;57(9):2612–2623. doi: 10.1128/iai.57.9.2612-2623.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Stamm L. V., Bassford P. J., Jr Cellular and extracellular protein antigens of Treponema pallidum synthesized during in vitro incubation of freshly extracted organisms. Infect Immun. 1985 Mar;47(3):799–807. doi: 10.1128/iai.47.3.799-807.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Swancutt M. A., Twehous D. A., Norgard M. V. Monoclonal antibody selection and analysis of a recombinant DNA-derived surface immunogen of Treponema pallidum expressed in Escherichia coli. Infect Immun. 1986 Apr;52(1):110–119. doi: 10.1128/iai.52.1.110-119.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Thornburg R. W., Baseman J. B. Comparison of major protein antigens and protein profiles of Treponema pallidum and Treponema pertenue. Infect Immun. 1983 Nov;42(2):623–627. doi: 10.1128/iai.42.2.623-627.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Walfield A. M., Roche E. S., Zounes M. C., Kirkpatrick H., Wild M. A., Textor G., Tsai P. K., Richardson C. Primary structure of an oligomeric antigen of Treponema pallidum. Infect Immun. 1989 Feb;57(2):633–635. doi: 10.1128/iai.57.2.633-635.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. van Embden J. D., van der Donk H. J., van Eijk R. V., van der Heide H. G., de Jong J. A., van Olderen M. F., Osterhaus A. B., Schouls L. M. Molecular cloning and expression of Treponema pallidum DNA in Escherichia coli K-12. Infect Immun. 1983 Oct;42(1):187–196. doi: 10.1128/iai.42.1.187-196.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]

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