Molecular characterization of receptor binding proteins and immunogens of virulent Treponema pallidum

J. B. Baseman, E. C. Hayes

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

Receptor binding proteins of Treponema pallidum were identified by incubation of [35S]methionine-labeled, soluble T. pallidum preparations with formaldehyde-fixed HEp-2 cells. Three major treponemal proteins (bands 1-3) that avidly bound to the eucaryotic cell surface were detected by sodium dodecylsulfate-polyacrylamide gel electrophoresis and fluorography. Brief trypsin treatment of HEp-2 cells before formaldehyde fixation reduced the extent of the interaction of these treponemal macromolecules, which implicated receptor-mediated attachment mechanisms. The presence of unlabeled T. pallidum preparations directly competed with radiolabeled T. pallidum samples for the available HEp-2 cells, which suggested a limiting number of membrane binding sites. Samples of unlabeled avirulent Reiter treponeme did not compete. T. pallidum immunogens were examined by radioimmunoprecipitation with human and rabbit syphilitic sera. Of interest were the similarities and extent of the humoral response represented by the detection of antigen-antibody complexes against numerous treponemal proteins, including bands 1-3. T. pallidum protein band 1 appeared to be the major antigenic stimulus. Formation of antigen-antibody complexes between 35S-labeled T. pallidum proteins and human syphilitic sera was prevented by unlabeled T. pallidum but not by T. phagedenis preparations, which demonstrated specificity of the reaction. Gel profiles of radioimmunoprecipitation assays using radiolabeled T. pallidum antigens and human syphilitic and yaws sera delineated both the similarities and differences in the humoral response to these two spirochetes. The latter suggested both overlapping and distinguishing antigenic properties between T. pallidum and T. pertenue. Detection in yaws sera of specific antibody against T. pallidum protein bands 1-3 further incriminates the role of these three treponemal proteins as virulence determinants.

Original languageEnglish (US)
Pages (from-to)573-586
Number of pages14
JournalJournal of Experimental Medicine
Volume151
Issue number3
StatePublished - 1980
Externally publishedYes

Fingerprint

Treponema pallidum
Carrier Proteins
Erythrocyte Anion Exchange Protein 1
Yaws
Antigen-Antibody Complex
Serum
Formaldehyde
Photofluorography
Proteins
Radioimmunoprecipitation Assay
Spirochaetales
Viral Tumor Antigens
Methionine
Trypsin
Virulence
Polyacrylamide Gel Electrophoresis
Gels
Sodium
Binding Sites
Rabbits

ASJC Scopus subject areas

  • Immunology

Cite this

Molecular characterization of receptor binding proteins and immunogens of virulent Treponema pallidum. / Baseman, J. B.; Hayes, E. C.

In: Journal of Experimental Medicine, Vol. 151, No. 3, 1980, p. 573-586.

Research output: Contribution to journalArticle

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