Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1983 Dec;42(3):1086–1091. doi: 10.1128/iai.42.3.1086-1091.1983

Enterobacterial common antigen-tetanus toxoid conjugate as immunogen.

C Lugowski, M Kułakowska, E Romanowska
PMCID: PMC264411  PMID: 6358039

Abstract

The methods of limited periodate oxidation and reductive amination were used to obtain covalently linked enterobacterial common antigen (ECA) with tetanus toxoid. This procedure is simple and gives a good yield of the conjugate with high ECA content (molecular ratio of ECA to tetanus toxoid, 6:1). The ECA-tetanus toxoid conjugate is immunogenic in rabbits, in contrast to free ECA or a mixture of ECA with proteins. This conjugate produces high levels of ECA-specific immunoglobulin G antibodies, which can be used as a standard serum.

Full text

PDF
1089

Images in this article

1088Image
on p.1088
1088Image
on p.1088
1089Image
on p.1089
1089Image
on p.1089

Selected References

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

  1. Avrameas S., Ternynck T. The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunoadsorbents. Immunochemistry. 1969 Jan;6(1):53–66. doi: 10.1016/0019-2791(69)90178-5. [DOI] [PubMed] [Google Scholar]
  2. Beuvery E. C., van Rossum F., Nagel J. Comparison of the induction of immunoglobulin M and G antibodies in mice with purified pneumococcal type 3 and meningococcal group C polysaccharides and their protein conjugates. Infect Immun. 1982 Jul;37(1):15–22. doi: 10.1128/iai.37.1.15-22.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Braley-Mullen H. Antigen requirements for priming of IgG producing B memory cells specific for Type III pneumococcal polysaccharide. Immunology. 1980 Aug;40(4):521–527. [PMC free article] [PubMed] [Google Scholar]
  4. Cuatrecasas P. Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads. J Biol Chem. 1970 Jun;245(12):3059–3065. [PubMed] [Google Scholar]
  5. Davie J. M., Paul W. E. Role of T lymphocytes in the humoral immune response. I. Proliferation of B lymphocytes in thymus-deprived mice. J Immunol. 1974 Nov;113(5):1438–1445. [PubMed] [Google Scholar]
  6. Dresser D. W., Popham A. M. The influence of T cells on the initiation and expression of immunological memory. Immunology. 1979 Oct;38(2):265–274. [PMC free article] [PubMed] [Google Scholar]
  7. Engvall E., Jonsson K., Perlmann P. Enzyme-linked immunosorbent assay. II. Quantitative assay of protein antigen, immunoglobulin G, by means of enzyme-labelled antigen and antibody-coated tubes. Biochim Biophys Acta. 1971 Dec 28;251(3):427–434. doi: 10.1016/0005-2795(71)90132-2. [DOI] [PubMed] [Google Scholar]
  8. Faulk W. P., Pondman K. W. Characterization of rabbit fast and slow 6-6S IgG. Immunochemistry. 1969 Mar;6(2):215–228. doi: 10.1016/0019-2791(69)90158-x. [DOI] [PubMed] [Google Scholar]
  9. Fielder R. J., Bishop C. T., Grappel S. F., Blank F. An immunogenic polysaccharide-protein conju- gate. J Immunol. 1970 Jul;105(1):265–267. [PubMed] [Google Scholar]
  10. Jennings H. J., Lugowski C. Immunochemistry of groups A, B, and C meningococcal polysaccharide-tetanus toxoid conjugates. J Immunol. 1981 Sep;127(3):1011–1018. [PubMed] [Google Scholar]
  11. Kiss P., Rinno J., Schmidt G., Mayer H. Structural studies on the immunogenic form of the enterobacterial common antigen. Eur J Biochem. 1978 Jul 17;88(1):211–218. doi: 10.1111/j.1432-1033.1978.tb12440.x. [DOI] [PubMed] [Google Scholar]
  12. Kuhn H. M., Adamus G., Romanowska E., Mayer H. Effect of proteins on the immunogenicity of enterobacterial common antigen. Infect Immun. 1981 Nov;34(2):373–377. doi: 10.1128/iai.34.2.373-377.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Ludowieg J., Benmaman J. D. Colorimetric differentiation of hexosamines. Anal Biochem. 1967 Apr;19(1):80–88. doi: 10.1016/0003-2697(67)90136-4. [DOI] [PubMed] [Google Scholar]
  15. Lugowski C., Romanowska E. Enterobacterial common antigen: isolation from Shigella sonnei, purification and immunochemical characterization. Eur J Biochem. 1978 Nov 2;91(1):89–97. doi: 10.1111/j.1432-1033.1978.tb20941.x. [DOI] [PubMed] [Google Scholar]
  16. Mayer H., Schmidt G. Chemistry and biology of the enterobacterial common antigen (ECA). Curr Top Microbiol Immunol. 1979;85:99–153. doi: 10.1007/978-3-642-67322-1_3. [DOI] [PubMed] [Google Scholar]
  17. Mechanic G., Gallop P. M., Tanzer M. L. The nature of crosslinking in collagens from mineralized tissues. Biochem Biophys Res Commun. 1971 Nov 5;45(3):644–653. doi: 10.1016/0006-291x(71)90465-7. [DOI] [PubMed] [Google Scholar]
  18. Mäkelä P. H., Mayer H. Enterobacterial common antigen. Bacteriol Rev. 1976 Sep;40(3):591–632. doi: 10.1128/br.40.3.591-632.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Männel D., Mayer H. Isolation and chemical characterization of the enterobacterial common antigen. Eur J Biochem. 1978 May 16;86(2):361–370. doi: 10.1111/j.1432-1033.1978.tb12318.x. [DOI] [PubMed] [Google Scholar]
  20. Männel D., Mayer H. Serological and immunological properties of isolated enterobacterial common antigen. Eur J Biochem. 1978 May 16;86(2):371–379. doi: 10.1111/j.1432-1033.1978.tb12319.x. [DOI] [PubMed] [Google Scholar]
  21. OUCHTERLONY O. Diffusion-in-gel methods for immunological analysis. II. Prog Allergy. 1962;6:30–154. doi: 10.1159/000313795. [DOI] [PubMed] [Google Scholar]
  22. Olson P. R., Weiblen B. J., O'Leary J. J., Moscowitz A. J., McCullough J. A simple technique for the inactivation of IgM antibodies using dithiothreitol. Vox Sang. 1976;30(2):149–159. doi: 10.1111/j.1423-0410.1976.tb02806.x. [DOI] [PubMed] [Google Scholar]
  23. Paul W. E., Katz D. H., Benacerraf B. Augmented anti-S 3 antibody responses to an S 3 -protein conjugate. J Immunol. 1971 Sep;107(3):685–688. [PubMed] [Google Scholar]
  24. Rinno J., Golecki J. R., Mayer H. Localization of enterobacterial common antigen:immunogenic and nonimmunogenic enterobacterial common antigen-containing Escherichia coli. J Bacteriol. 1980 Feb;141(2):814–821. doi: 10.1128/jb.141.2.814-821.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Romanowska E., Mulczyk M. Chemical studies on the specific fragment of Shigella sonnei phase II. Eur J Biochem. 1968 Jun;5(1):109–113. doi: 10.1111/j.1432-1033.1968.tb00343.x. [DOI] [PubMed] [Google Scholar]
  26. Schwartz B. A., Gray G. R. Proteins containing reductively aminated disaccharides. Synthesis and chemical characterization. Arch Biochem Biophys. 1977 Jun;181(2):542–549. doi: 10.1016/0003-9861(77)90261-2. [DOI] [PubMed] [Google Scholar]
  27. Svenson S. B., Lindberg A. A. Immunochemistry of Salmonella O-antigens: preparation of an octasaccharide-bovine serum albumin immunogen representative of Salmonella serogroup B O-antigen and characterization of the antibody response. J Immunol. 1978 May;120(5):1750–1757. [PubMed] [Google Scholar]
  28. Voller A., Draper C., Bidwell D. E., Bartlett A. Microplate enzyme-linked immunosorbent assay for chagas' disease. Lancet. 1975 Feb 22;1(7904):426–428. doi: 10.1016/s0140-6736(75)91492-0. [DOI] [PubMed] [Google Scholar]
  29. Weeke B. Crossed immunoelectrophoresis. Scand J Immunol Suppl. 1973;1:47–56. doi: 10.1111/j.1365-3083.1973.tb03778.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES