Skip to main content
NCBI home page
Journal of Clinical Microbiology logoLink to Journal of Clinical Microbiology
. 1981 Jul;14(1):32–38. doi: 10.1128/jcm.14.1.32-38.1981

Ethylenediaminetetraacetic acid (disodium salt)-labile bovine immunoglobulin M Fc binding to Brucella abortus: a cause of nonspecific agglutination.

K Nielsen, K Stilwell, B Stemshorn, R Duncan
PMCID: PMC271898  PMID: 6790568

Abstract

It was demonstrated by a radioimmunoassay procedure that Brucella abortus agglutinins from noninfected cattle sera, absorbed to B. abortus antigen and eluted with ethylenediaminetetraacetic acid (EDTA), was immunoglobulin M that bound to that bacterium by its Fc portion. The EDTA-eluted immunoglobulin M agglutinated intact B. abortus cells but not erythrocytes treated with B. abortus lipopolysaccharide. The specificity of the EDTA-eluted immunoglobulin was for B. abortus, although a small titer to Yersinia enterocolitica serotype O:9 was observed. In contrast, immunoglobulin M purified from the serum of a cow injected 7 days previously with heat-killed B. abortus bound to the antigen by its Fab portion, was not labile to EDTA treatment, cross-reacted extensively with Y. enterocolitica serotype O:9, and agglutinated various other bacterial antigens and normal erythrocytes.

Full text

PDF
32

Images in this article

33Image
on p.33

Selected References

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

  1. Ashwell G., Morell A. G. The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Adv Enzymol Relat Areas Mol Biol. 1974;41(0):99–128. doi: 10.1002/9780470122860.ch3. [DOI] [PubMed] [Google Scholar]
  2. Baker P. J., Wilson J. B. Hypoferremia in mice and its application to the bioassay of endotoxin. J Bacteriol. 1965 Oct;90(4):903–910. doi: 10.1128/jb.90.4.903-910.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Barta O., Barta V. Haemolytic assay of bovine serum complement. J Immunol Methods. 1972 Aug;1(4):363–374. doi: 10.1016/0022-1759(72)90029-4. [DOI] [PubMed] [Google Scholar]
  4. Cochrane C. G., Müller-Eberhard H. J., Aikin B. S. Depletion of plasma complement in vivo by a protein of cobra venom: its effect on various immunologic reactions. J Immunol. 1970 Jul;105(1):55–69. [PubMed] [Google Scholar]
  5. Delacroix D., Vaerman J. P. Simple purification of goat IgG1 and IgG2 subclasses by chromatography on protein A-sepharose at various pH. Mol Immunol. 1979 Oct;16(10):837–840. doi: 10.1016/0161-5890(79)90164-0. [DOI] [PubMed] [Google Scholar]
  6. Diaz R., Jones L. M., Leong D., Wilson J. B. Differences between Brucella antigens involved in indirect hemagglutination tests with normal and tanned red blood cells. J Bacteriol. 1967 Sep;94(3):499–505. doi: 10.1128/jb.94.3.499-505.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Duhamel R. C., Meezan E., Brendel K. The pH-dependent binding of goat IgG1 and IgG2 to protein A-sepharose. Mol Immunol. 1980 Jan;17(1):29–36. doi: 10.1016/0161-5890(80)90121-2. [DOI] [PubMed] [Google Scholar]
  8. Fey H. A simple procedure for the production of Fab from bovine IgG as an absorbent in the preparation of class-specific anti-immunoglobulin. Immunochemistry. 1975 Mar;12(3):235–239. doi: 10.1016/0019-2791(75)90237-2. [DOI] [PubMed] [Google Scholar]
  9. Forsgren A., Sjöquist J. "Protein A" from S. aureus. I. Pseudo-immune reaction with human gamma-globulin. J Immunol. 1966 Dec;97(6):822–827. [PubMed] [Google Scholar]
  10. Goudswaard J., van der Donk J. A., Noordzij A., van Dam R. H., Vaerman J. P. Protein A reactivity of various mammalian immunoglobulins. Scand J Immunol. 1978;8(1):21–28. doi: 10.1111/j.1365-3083.1978.tb00492.x. [DOI] [PubMed] [Google Scholar]
  11. Grey H. M., Kohler P. F. Cryoimmunoglobulins. Semin Hematol. 1973 Apr;10(2):87–112. [PubMed] [Google Scholar]
  12. HESS W. R., ROEPKE M. H. A non-specific Brucella agglutinating substance in bovine serum. Proc Soc Exp Biol Med. 1951 Jul;77(3):469–472. doi: 10.3181/00379727-77-18817. [DOI] [PubMed] [Google Scholar]
  13. HESS W. R. Studies on a nonspecific Brucella-agglutinating substance in bovin serum. I. The differentiation of the specific and nonspecific agglutinins by heat treatment. Am J Vet Res. 1953 Apr;14(51):192–194. [PubMed] [Google Scholar]
  14. HESS W. R. Studies on a nonspecific Brucella-agglutinating substance in bovine serum. II. Isolation and purification of the Brucella-agglutinating substances. Am J Vet Res. 1953 Apr;14(51):195–197. [PubMed] [Google Scholar]
  15. Hurvell B., Lindberg A. A. Serological cross-reactions between different Brucella species and Yersinia enterocolitica. Immunochemical studies on phenol-water extracted lipopolysaccharides from Brucella abortus and Yersinia enterocolitica type IX. Acta Pathol Microbiol Scand B Microbiol Immunol. 1973 Feb;81(1):113–119. [PubMed] [Google Scholar]
  16. Kronvall G. A surface component in group A, C, and G streptococci with non-immune reactivity for immunoglobulin G. J Immunol. 1973 Nov;111(5):1401–1406. [PubMed] [Google Scholar]
  17. Lamb V. L., Jones L. M., Schurig G. G., Berman D. T. Enzyme-linked immunosorbent assay for bovine immunoglobulin subclass-specific response to Brucella abortus lipopolysaccharides. Infect Immun. 1979 Oct;26(1):240–247. doi: 10.1128/iai.26.1.240-247.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Levo Y. Nature of cryoglobulinaemia. Lancet. 1980 Feb 9;1(8163):285–287. doi: 10.1016/s0140-6736(80)90781-3. [DOI] [PubMed] [Google Scholar]
  19. McConahey P. J., Dixon F. J. A method of trace iodination of proteins for immunologic studies. Int Arch Allergy Appl Immunol. 1966;29(2):185–189. doi: 10.1159/000229699. [DOI] [PubMed] [Google Scholar]
  20. Morgan W. J. The serological diagnosis of bovine brucellosis. Vet Rec. 1967 May 27;80(21):612–620. doi: 10.1136/vr.80.21.612. [DOI] [PubMed] [Google Scholar]
  21. Nielsen K. Preparation of antisera to the mu chain of IgM. J Immunol Methods. 1976;11(1):77–82. doi: 10.1016/0022-1759(76)90020-x. [DOI] [PubMed] [Google Scholar]
  22. Nielsen K., Samagh B. S., Speckmann G., Stemshorn B. The bovine immune response to Brucella abortus. II. Elimination of some sporadic serological reactions by chelation of divalent cations. Can J Comp Med. 1979 Oct;43(4):420–425. [PMC free article] [PubMed] [Google Scholar]
  23. OUCHTERLONY O. Antigen-antibody reactions in gels. IV. Types of reactions in coordinated systems of diffusion. Acta Pathol Microbiol Scand. 1953;32(2):230–240. [PubMed] [Google Scholar]
  24. Onoue K., Kishimoto T., Yamamura Y. Papain fragmentation of the subunits of human macroglobulin. J Immunol. 1967 Feb;98(2):303–313. [PubMed] [Google Scholar]
  25. Parratt D., Nielsen K. H., White R. G. Radioimmunoassay of IgM, IgG, and IgA Brucella antibodies. Lancet. 1977 May 21;1(8021):1075–1078. doi: 10.1016/s0140-6736(77)92334-0. [DOI] [PubMed] [Google Scholar]
  26. ROSE J. E., LAMBERT G., ROEPKE M. H. ULTRACENTRIFUGATION AND HEAT-INACTIVATION STUDIES ON SEROAGGLUTININS OF PREGNANT HEIFERS ARTIFICIALLY INFECTED WITH VIRULENT BRUCELLA ABORTUS. Am J Vet Res. 1964 Mar;25:329–332. [PubMed] [Google Scholar]
  27. ROSE J. E., ROEPKE M. H. An acidified antigen for detection of nonspecific reactions in the plate-agglutination test for bovine brucellosis. Am J Vet Res. 1957 Jul;18(68):550–555. [PubMed] [Google Scholar]
  28. ROSE J. E., ROEPKE M. H., BRIGGS D. R. PHYSICOCHEMICAL PROPERTIES OF NONSPECIFIC BOVINE SEROAGGLUTININS FOR BRUCELLA ABORTUS. Am J Vet Res. 1964 Jan;25:118–121. [PubMed] [Google Scholar]
  29. ROSE J. E., ROEPKE M. H. PHYSICOCHEMICAL STUDIES ON POSTVACCINAL BRUCELLA AGGLUTININS IN BOVINE SERUM. Am J Vet Res. 1964 Mar;25:325–328. [PubMed] [Google Scholar]
  30. SCHEIDEGGER J. J. Une micro-méthode de l'immuno-electrophorèse. Int Arch Allergy Appl Immunol. 1955;7(2):103–110. [PubMed] [Google Scholar]
  31. Stephens C. G., Reed W. P., Kronvall G., Williams R. C., Jr Reactions between certain strains of pneumococci and Fc of IgG. J Immunol. 1974 Jun;112(6):1955–1960. [PubMed] [Google Scholar]
  32. Zikán J., Miler I. The in vivo opsonizing activity of Fab mu and F(c)5 mu fragments of pig immunoglobulin M to Escherichia coli 0 55 in newborn, precolostral piglets. Immunochemistry. 1975 Oct;12(10):813–815. doi: 10.1016/0019-2791(75)90145-7. [DOI] [PubMed] [Google Scholar]

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

RESOURCES