Skip to main content
PMC home page
The British Journal of Venereal Diseases logoLink to The British Journal of Venereal Diseases
. 1983 Apr;59(2):75–79. doi: 10.1136/sti.59.2.75

Enzyme-linked immunosorbent assay for the detection of serum antibody to outer membrane proteins of Treponema pallidum.

J Morrison-Plummer, J F Alderete, J B Baseman
PMCID: PMC1046140  PMID: 6339000

Abstract

A highly sensitive enzyme-linked immunosorbent assay was used for the analysis of serum IgG reactivity against specific immunogenic Treponema pallidum proteins. Outer membrane treponemal proteins purified by preparative SDS-polyacrylamide gel electrophoresis were used as antigenic probes at concentrations as low as 100 ng per ml (5 ng per well in microtitre plates). Detection of anti-treponemal antibody was possible using rabbit syphilitic sera diluted to 1/10 000. The sensitivity of the assay was equal to or greater than that detected by radioimmuno-precipitation combined with gel electrophoresis and fluorography techniques and was capable of monitoring host IgG responses throughout the progress of the disease.

Full text

PDF
75

Images in this article

77Image
on p.77

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  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. Alderete J. F., Baseman J. B. Surface characterization of virulent Treponema pallidum. Infect Immun. 1980 Dec;30(3):814–823. doi: 10.1128/iai.30.3.814-823.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Alderete J. F., Baseman J. B. Surface-associated host proteins on virulent Treponema pallidum. Infect Immun. 1979 Dec;26(3):1048–1056. doi: 10.1128/iai.26.3.1048-1056.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  6. Cobbold S. P., Waldmann H. A rapid solid-phase enzyme-linked binding assay for screening monoclonal antibodies to cell surface antigens. J Immunol Methods. 1981;44(2):125–133. doi: 10.1016/0022-1759(81)90340-9. [DOI] [PubMed] [Google Scholar]
  7. Douillard J. Y., Hoffman T., Herberman R. B. Enzyme-linked immunosorbent assay for screening monoclonal antibody production: use of intact cells as antigen. J Immunol Methods. 1980;39(4):309–316. doi: 10.1016/0022-1759(80)90231-8. [DOI] [PubMed] [Google Scholar]
  8. Garner M. F., Backhouse J. L. Chronic biological false-positive reactions to serological tests for syphilis in blood donors. J Clin Pathol. 1970 Sep;23(6):478–480. doi: 10.1136/jcp.23.6.478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Horowitz S. A., Cassell G. H. Detection of antibodies to Mycoplasma pulmonis by an enzyme-linked immunosorbent assay. Infect Immun. 1978 Oct;22(1):161–170. doi: 10.1128/iai.22.1.161-170.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Le Clair R. A., Montague T. S., Keetin L. M. Biologic false-positive reactions for syphilis as measured by the Treponema pallidum immobilization test. J Med. 1972;3(4):264–269. [PubMed] [Google Scholar]
  11. Luger A., Schmidt B. L., Spendlingwimmer I., Steyrer K. Specificity of the Treponema pallidum haemagglutination test. Analysis of results. Br J Vener Dis. 1981 Jun;57(3):178–180. doi: 10.1136/sti.57.3.178. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Nell E. E., Hardy P. H., Jr The use of freeze-preserved treponemes in the Treponema pallidum immobilization test. Cryobiology. 1972 Oct;9(5):404–410. doi: 10.1016/0011-2240(72)90157-5. [DOI] [PubMed] [Google Scholar]
  13. Pepose J. S., Bishop N. H., Feigenbaum S., Miller J. N., Zeltzer P. M. 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. Sex Transm Dis. 1980 Jul-Sep;7(3):125–129. [PubMed] [Google Scholar]
  14. Pien F. D., Markowitz H., McKenna C. H., Schroeter A. L. Problems with beaded fluorescence pattern in FTA-ABS test. J Am Vener Dis Assoc. 1976 Sep;3(1):20–24. [PubMed] [Google Scholar]
  15. Rathlev T. Haemagglutination test utilizing pathogenic Treponema pallidum for the sero-diagnosis of syphilis. Br J Vener Dis. 1967 Sep;43(3):181–185. doi: 10.1136/sti.43.3.181. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Roehrig J. T., Corser J. A., Schlesinger M. J. Isolation and characterization of hybrid cell lines producing monoclonal antibodies directed against the structural proteins of Sindbis virus. Virology. 1980 Feb;101(1):41–49. doi: 10.1016/0042-6822(80)90481-x. [DOI] [PubMed] [Google Scholar]
  17. Zeltzer P. M., Pepose J. S., Bishop N. H., Miller J. N. Microassay for immunoglobulin G antibodies to Treponema pallidum with radioiodinated protein A from staphylococcus aureus: immunoglobulin G response in experimental syphilis in rabbits. Infect Immun. 1978 Jul;21(1):163–170. doi: 10.1128/iai.21.1.163-170.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from British Journal of Venereal Diseases are provided here courtesy of BMJ Publishing Group

RESOURCES