Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1979 Dec;26(3):1048–1056. doi: 10.1128/iai.26.3.1048-1056.1979

Surface-Associated Host Proteins on Virulent Treponema pallidum

John F Alderete 1, Joel B Baseman 1
PMCID: PMC414726  PMID: 93574

Abstract

A surface coat of host serum proteins was detected on virulent Treponema pallidum by sodium dodecyl sulfate-gel electrophoresis. The loosely associated serum proteins could be removed by repeated washings in a protein-free medium. Washed T. pallidum retained the ability to readsorb numerous host proteins from rabbit serum as well as iodinated rabbit or human albumin. In addition, various avidly associated host serum proteins including albumin, α2-macroglobulin, transferrin, ceruloplasmin, immunoglobulin G, immunoglobulin M, and C3 were identified on the outer envelope of washed treponemes by an immunoadsorbent technique with protein A-bearing staphylococcus. Hyaluronidase treatment did not remove the avidly associated host proteins from the surface of washed treponemes, whereas trypsin treatment resulted in decreased levels of agglutination. Electrophoretic patterns of trypsin-treated treponemes showed that treponemal proteins as well as adsorbed host proteins were released concurrently by protease digestion. Reacquisition studies involving α2-macroglobulin and transferrin suggested the presence of noncompetitive binding sites for serum proteins on the treponemal outer envelope. Finally, differences among the T. pallidum preparations from individual rabbits with respect to incorporation of [35S]methionine, extent of agglutination with antisera, and length of time required for removal of avidly associated host proteins by trypsin treatment indicated biological variability among the treponemal populations.

Full text

PDF
1048

Images in this article

1050Image
on p.1050
1051Image
on p.1051
1053Image
on p.1053

Selected References

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

  1. Allsopp B. A., Njogu A. R. Monosaccharide composition of the surface glycoprotein antigens of Trypanosoma brucei. Parasitology. 1974 Dec;69(3):271–281. doi: 10.1017/s0031182000062971. [DOI] [PubMed] [Google Scholar]
  2. Baseman J. B., Hayes N. S. Protein synthesis by Treponema pallidum extracted from infected rabbit tissue. Infect Immun. 1974 Dec;10(6):1350–1355. doi: 10.1128/iai.10.6.1350-1355.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Baseman J. B., Nichols J. C., Mogerley S. Capacity of virulent Treponema pallidum (Nichols) for deoxyribonucleic acid synthesis. Infect Immun. 1979 Feb;23(2):392–397. doi: 10.1128/iai.23.2.392-397.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Baseman J. B., Nichols J. C., Rumpp J. W., Hayes N. S. Purification of Treponema pallidum from Infected Rabbit Tissue: Resolution into Two Treponemal Populations. Infect Immun. 1974 Nov;10(5):1062–1067. doi: 10.1128/iai.10.5.1062-1067.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  6. Brause B. D., Roberts R. B. Attachment of virulent Treponema pallidum to human mononuclear phagocytes. Br J Vener Dis. 1978 Aug;54(4):218–224. doi: 10.1136/sti.54.4.218. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. CHRISTIANSEN S. Protective layer covering pathogenic treponemata. Lancet. 1963 Feb 23;1(7278):423–425. doi: 10.1016/s0140-6736(63)92309-2. [DOI] [PubMed] [Google Scholar]
  8. Cross G. A. Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei. Parasitology. 1975 Dec;71(3):393–417. doi: 10.1017/s003118200004717x. [DOI] [PubMed] [Google Scholar]
  9. Diffley P. Comparative immunological analysis of host plasma proteins bound to bloodstream forms of Trypanosoma brucei subspecies. Infect Immun. 1978 Aug;21(2):605–612. doi: 10.1128/iai.21.2.605-612.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Dwyer D. M. Immunologic and fine structure evidence of avidly bound host serum proteins in the surface coat of a bloodstream trypanosome. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1222–1226. doi: 10.1073/pnas.73.4.1222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fieldsteel A. H., Becker F. A., Stout J. G. Prolonged survival of virulent Treponema pallidum (Nichols strain) in cell-free and tissue culture systems. Infect Immun. 1977 Oct;18(1):173–182. doi: 10.1128/iai.18.1.173-182.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Fieldsteel A. H., Stout J. G., Becker F. A. Comparative behavior of virulent strains of Treponema pallidum and Treponema pertenue in gradient cultures of various mammalian cells. Infect Immun. 1979 May;24(2):337–345. doi: 10.1128/iai.24.2.337-345.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Fitzgerald T. J., Johnson R. C. Surface mucopolysaccharides of Treponema pallidum. Infect Immun. 1979 Apr;24(1):244–251. doi: 10.1128/iai.24.1.244-251.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Giannini M. S., D'Alesandro P. A. Unusual antibody-induced modulation of surface antigens in the cell coat of a bloodstream trypanosome. Science. 1978 Sep 8;201(4359):916–918. doi: 10.1126/science.356265. [DOI] [PubMed] [Google Scholar]
  15. Griffin F. M., Jr, Griffin J. A., Leider J. E., Silverstein S. C. Studies on the mechanism of phagocytosis. I. Requirements for circumferential attachment of particle-bound ligands to specific receptors on the macrophage plasma membrane. J Exp Med. 1975 Nov 1;142(5):1263–1282. doi: 10.1084/jem.142.5.1263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hayes N. S., Muse K. E., Collier A. M., Baseman J. B. Parasitism by virulent Treponema pallidum of host cell surfaces. Infect Immun. 1977 Jul;17(1):174–186. doi: 10.1128/iai.17.1.174-186.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hu P. C., Collier A. M., Baseman J. B. Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium. J Exp Med. 1977 May 1;145(5):1328–1343. doi: 10.1084/jem.145.5.1328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Jones R. H., Finn M. A., Thomas J. J., Folger C. Growth and subculture of pathogenic T. pallidum (Nichols strain) in BHK-21 cultured tissue cells. Br J Vener Dis. 1976 Feb;52(1):18–23. doi: 10.1136/sti.52.1.18. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Jones R. H., Nevin T. A., Guest W. J., Logan L. C. Lytic effect of trypsin, lysozyme, and complement on Treponema pallidum. Br J Vener Dis. 1968 Sep;44(3):193–200. doi: 10.1136/sti.44.3.193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kessler S. W. Cell membrane antigen isolation with the staphylococcal protein A-antibody adsorbent. J Immunol. 1976 Nov;117(5 Pt 1):1482–1490. [PubMed] [Google Scholar]
  21. METZGER M., HARDY P. H., Jr, NELL E. E. Influence of lysozyme upon the treponeme immobilization reaction. Am J Hyg. 1961 Mar;73:236–244. doi: 10.1093/oxfordjournals.aje.a120182. [DOI] [PubMed] [Google Scholar]
  22. Mayer M. M., Hammer C. H., Michaels D. W., Shin M. L. Immunologically mediated membrane damage: the mechanism of complement action and the similarity of lymphocyte-mediated cytoxicity. Immunochemistry. 1978 Nov;15(10-11):813–831. doi: 10.1016/0161-5890(78)90115-3. [DOI] [PubMed] [Google Scholar]
  23. Nagle R. B., Ward P. A., Lindsley H. B., Sadun E. H., Johnson A. J., Berkaw R. E., Hildebrandt P. K. Experimental infections with African Trypanosomes. VI. Glomerulonephritis involving the alternate pathway of complement activation. Am J Trop Med Hyg. 1974 Jan;23(1):15–26. [PubMed] [Google Scholar]
  24. 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]
  25. Nichols J. C., Baseman J. B. Ribosomal ribonucleic acid synthesis by virulent Treponema pallidum. Infect Immun. 1978 Mar;19(3):854–860. doi: 10.1128/iai.19.3.854-860.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. PELTIER A., CHRISTIAN C. L. The presence of the rheumatoid factor in sera from patients with syphilis. Arthritis Rheum. 1959 Feb;2(1):1–7. doi: 10.1002/1529-0131(195902)2:1<1::aid-art1780020102>3.0.co;2-d. [DOI] [PubMed] [Google Scholar]
  27. Sandok P. L., Jenkin H. M., Matthews H. M., Roberts M. S. Unsustained multiplication of treponema pallidum (nichols virulent strain) in vitro in the presence of oxygen. Infect Immun. 1978 Feb;19(2):421–429. doi: 10.1128/iai.19.2.421-429.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Schiller N. L., Cox C. D. Catabolism of glucose and fatty acids by virulent Treponema pallidum. Infect Immun. 1977 Apr;16(1):60–68. doi: 10.1128/iai.16.1.60-68.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Torpier G., Capron A., Ouaissi M. A. Receptor for IgG(Fc) and human beta2-microglobulin on S. mansoni schistosomula. Nature. 1979 Mar 29;278(5703):447–449. doi: 10.1038/278447a0. [DOI] [PubMed] [Google Scholar]
  30. Zeigler J. A., Jones A. M., Jones R. H., Kubica K. M. Demonstration of extracellular material at the surface of pathogenic T. pallidum cells. Br J Vener Dis. 1976 Feb;52(1):1–8. doi: 10.1136/sti.52.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES