Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1986 Mar;165(3):732–739. doi: 10.1128/jb.165.3.732-739.1986

Properties of an ordered ring structure formed by recombinant Treponema pallidum surface antigen 4D.

T E Fehniger, J D Radolf, M A Lovett
PMCID: PMC214490  PMID: 3512520

Abstract

Ultrastructural and biochemical studies of a recombinant Treponema pallidum surface antigen designated 4D have been conducted due to its likely biological significance. Electron microscopy demonstrated that the 190-kilodalton (kDa) 4D molecule is an ordered ring structure of 10-nm diameter. The 90-kDa proteinase K-treated 4D is an ordered ring structure of 6-nm diameter. Evidence is presented that the 190-kDa ordered ring is maintained by noncovalent bonds; 19-kDa monomers can reassociate in vitro to reform a 190-kDa molecule. Amino acid composition analysis of 190-kDa 4D showed that the molecule is composed of 45% hydrophobic residues. Evidence relating the structure of the 4D ordered ring to its potential role in the pathogenesis of syphilis is discussed.

Full text

PDF
732

Images in this article

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. 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]
  2. 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]
  3. BITTER T., MUIR H. M. A modified uronic acid carbazole reaction. Anal Biochem. 1962 Oct;4:330–334. doi: 10.1016/0003-2697(62)90095-7. [DOI] [PubMed] [Google Scholar]
  4. Bavoil P., Ohlin A., Schachter J. Role of disulfide bonding in outer membrane structure and permeability in Chlamydia trachomatis. Infect Immun. 1984 May;44(2):479–485. doi: 10.1128/iai.44.2.479-485.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  6. Chen R., Krämer C., Schmidmayr W., Henning U. Primary structure of major outer membrane protein I of Escherichia coli B/r. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5014–5017. doi: 10.1073/pnas.76.10.5014. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chen R., Schmidmayr W., Krämer C., Chen-Schmeisser U., Henning U. Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4592–4596. doi: 10.1073/pnas.77.8.4592. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Eshdat Y., Silverblatt F. J., Sharon N. Dissociation and reassembly of Escherichia coli type 1 pili. J Bacteriol. 1981 Oct;148(1):308–314. doi: 10.1128/jb.148.1.308-314.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hanff P. A., Norris S. J., Lovett M. A., Miller J. N. Purification of Treponema pallidum, Nichols strain, by Percoll density gradient centrifugation. Sex Transm Dis. 1984 Oct-Dec;11(4):275–286. doi: 10.1097/00007435-198410000-00003. [DOI] [PubMed] [Google Scholar]
  10. Hovind-Hougen K., Birch-Andersen A., Nielsen H. A. Electron microscopy of treponemes subjected to the Treponema pallidum immobilization (TPI) test. II. Immunoelectron microscopy. Acta Pathol Microbiol Scand C. 1979 Aug;87C(4):263–268. [PubMed] [Google Scholar]
  11. Jourdian G. W., Dean L., Roseman S. The sialic acids. XI. A periodate-resorcinol method for the quantitative estimation of free sialic acids and their glycosides. J Biol Chem. 1971 Jan 25;246(2):430–435. [PubMed] [Google Scholar]
  12. Klein J. R., Monjan A. A., Hardy P. H., Jr, Cole G. A. Abrogation of genetically controlled resistance of mice to Treponema pallidum by irradiation. Nature. 1980 Feb 7;283(5747):572–574. doi: 10.1038/283572a0. [DOI] [PubMed] [Google Scholar]
  13. LEVVY G. A., MCALLAN A. The N-acetylation and estimation of hexosamines. Biochem J. 1959 Sep;73:127–132. doi: 10.1042/bj0730127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. Lugtenberg B., Van Alphen L. Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria. Biochim Biophys Acta. 1983 Mar 21;737(1):51–115. doi: 10.1016/0304-4157(83)90014-x. [DOI] [PubMed] [Google Scholar]
  16. Marchalonis J. J. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem J. 1969 Jun;113(2):299–305. doi: 10.1042/bj1130299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. Nakae T., Ishii J., Tokunaga M. Subunit structure of functional porin oligomers that form permeability channels in the other membrane of Escherichia coli. J Biol Chem. 1979 Mar 10;254(5):1457–1461. [PubMed] [Google Scholar]
  19. 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]
  20. OSBORN M. J. STUDIES ON THE GRAM-NEGATIVE CELL WALL. I. EVIDENCE FOR THE ROLE OF 2-KETO- 3-DEOXYOCTONATE IN THE LIPOPOLYSACCHARIDE OF SALMONELLA TYPHIMURIUM. Proc Natl Acad Sci U S A. 1963 Sep;50:499–506. doi: 10.1073/pnas.50.3.499. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. 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]
  22. Valentine R. C., Shapiro B. M., Stadtman E. R. Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli. Biochemistry. 1968 Jun;7(6):2143–2152. doi: 10.1021/bi00846a017. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES