Skip to main content
NCBI home page
Infection and Immunity logoLink to Infection and Immunity
. 1980 Jul;29(1):50–58. doi: 10.1128/iai.29.1.50-58.1980

Complement activation induced by rabbit rheumatoid factor.

R R Meyer, J C Brown
PMCID: PMC551073  PMID: 7399707

Abstract

Rabbit rheumatoid factor produced in animals by hyperimmunized with group C streptococcal vaccine activated guinea pig complement. Anti-streptococcal serum was fractionated by Sephacryl S-200 chromatography into excluded (19S) and included (7S) material and examined for hemolytic activity in a sensitive homologous hemolytic assay system. In the presence of complement, both 19S and 7S antistreptococcal serum fractions induced lysis of bovine (ox) erythrocytes coated with mildly reduced and carboxymethylated rabbit anti-erythrocyte immunoglobulin G. That rabbit rheumatoid factor was responsible for the observed hemolytic activity was substantiated by hemolytic inhibition assays. Significant inhibition of hemolysis was effected when antistreptococcal serum fractions were incubated in the presence of human immunoglobulin G, rabbit immunoglobulin G, and Fc, whereas, no inhibition was detected when the same fractions were tested in the presence of rabbit Fab or F(ab')2 fragments. Deaggregation of inhibitor preparations revealed a preferential reactivity of rheumatoid factor for rabbit immunoglobulin G. In addition to the rheumatoid factor-dependent hemolytic activity observed in humoral preparations, immunoglobulin G-specific antibody-forming cells in spleen and peripheral blood lymphocyte isolates were enumerated by plaque-forming cell assay.

Full text

PDF
50

Selected References

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

  1. Bokisch V. A., Bernstein D., Krause R. M. Occurrence of 19S and 7S anti-IgGs during hyperimmunization of rabbits with streptococci. J Exp Med. 1972 Oct 1;136(4):799–815. doi: 10.1084/jem.136.4.799. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bokisch V. A., Chiao J. W., Bernstein D., Krause R. M. Homogenous rabbit 7S anti-IgG with antibody specificity for peptidoglycan. J Exp Med. 1973 Nov 1;138(5):1184–1193. doi: 10.1084/jem.138.5.1184. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brown J. C., Koshland M. E. Activation of antibody Fc function by antigen-induced conformational changes. Proc Natl Acad Sci U S A. 1975 Dec;72(12):5111–5115. doi: 10.1073/pnas.72.12.5111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brown J. C., Koshland M. E. Evidence for a long-range conformational change induced by antigen binding to IgM antibody. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5682–5686. doi: 10.1073/pnas.74.12.5682. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Brown J. C., Rodkey L. S. Autoregulation of an antibody response via network-induced auto-anti-idiotype. J Exp Med. 1979 Jul 1;150(1):67–85. doi: 10.1084/jem.150.1.67. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bøyum A. Isolation of lymphocytes, granulocytes and macrophages. Scand J Immunol. 1976 Jun;Suppl 5:9–15. [PubMed] [Google Scholar]
  7. Chiang H. C., Koshland M. E. Antigen-induced conformational changes in IgM antibody. I. The role of the antigenic determinant. J Biol Chem. 1979 Apr 25;254(8):2736–2741. [PubMed] [Google Scholar]
  8. Chiang H. C., Koshland M. E. Antigen-induced conformational changes in IgM antibody. II. The role of the carrier. J Biol Chem. 1979 Apr 25;254(8):2742–2747. [PubMed] [Google Scholar]
  9. Chiao J. W., Bokisch V. A., Christian C. L., Krause R. M. A rabbit IgG antigenic marker detected by 19S anti-IgG present in streptococcal antisera. J Immunol. 1974 Feb;112(2):627–632. [PubMed] [Google Scholar]
  10. Coligan J. E., Fraser B. A., Kindt T. J. A disaccharide hapten from streptococcal group C carbohydrate that cross-reacts with the Forssman glycolipid. J Immunol. 1977 Jan;118(1):6–11. [PubMed] [Google Scholar]
  11. Colling R. G., Brown J. C. The appearance of IgM and IgG cold agglutinins in rabbits hyperimmunized with group C streptococcal vaccine. J Immunol. 1979 Jan;122(1):202–208. [PubMed] [Google Scholar]
  12. Cunningham A. J. A method of increased sensitivity for detecting single antibody-forming cells. Nature. 1965 Sep 4;207(5001):1106–1107. doi: 10.1038/2071106a0. [DOI] [PubMed] [Google Scholar]
  13. Cunningham A. J., Szenberg A. Further improvements in the plaque technique for detecting single antibody-forming cells. Immunology. 1968 Apr;14(4):599–600. [PMC free article] [PubMed] [Google Scholar]
  14. DRESNER E., TROMBLY P. The latex-fixation reaction in nonrheumatic diseases. N Engl J Med. 1959 Nov 12;261:981–988. doi: 10.1056/NEJM195911122612001. [DOI] [PubMed] [Google Scholar]
  15. Dresser D. W. Most IgM-producing cells in the mouse secrete auto-antibodies (rheumatoid factor). Nature. 1978 Aug 3;274(5670):480–483. doi: 10.1038/274480a0. [DOI] [PubMed] [Google Scholar]
  16. Gipson T. G., Daniels C. A. The effect of rheumatoid factor on the immune lysis of vaccinia virus-infected cells. Clin Immunol Immunopathol. 1975 May;4(1):16–23. doi: 10.1016/0090-1229(75)90034-3. [DOI] [PubMed] [Google Scholar]
  17. HEIMER R., LEVIN F. M., KAHN M. F. INHIBITION OF COMPLEMENT FIXATION BY HUMAN SERUM. II. THE ACTIVITY OF A GAMMA-LM GLOBULIN AND RHEUMATOID FACTOR IN COMPLEMENT FIXATION REACTIONS. J Immunol. 1963 Dec;91:866–872. [PubMed] [Google Scholar]
  18. Hamers R., Hamers-Casterman C., van der Loo W., Strosberg A. D., De Baetselier P. Rheumatoid factor appearance in Micrococcus lysodeikticus immunization and its interference with allotype specific reactions. Z Immunitatsforsch Exp Klin Immunol. 1975 Jul;149(2-4):187–192. [PubMed] [Google Scholar]
  19. Houba V., Allison A. C. M-antiglobulins (rheumatoid-factor-like globulins) and other gamma-globulins in relation to tropical parasitic infections. Lancet. 1966 Apr 16;1(7442):848–852. doi: 10.1016/s0140-6736(66)90186-3. [DOI] [PubMed] [Google Scholar]
  20. Hurst M. M., Volanakis J. E., Stroud R. M., Bennett J. C. A comparative analysis of the C1-binding ability of fragments derived from complement-fixing and noncomplement-fixing IgM proteins. J Clin Invest. 1976 Jul;58(1):16–21. doi: 10.1172/JCI108445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Keeler K. D., Phillips J. M., Dresser D. W. IgM rheumatoid factor as a source of non-specificity in murine anti-allotype sera. Immunology. 1979 May;37(1):263–271. [PMC free article] [PubMed] [Google Scholar]
  22. Krause R. M. The search for antibodies with molecular uniformity. Adv Immunol. 1970;12:1–56. doi: 10.1016/s0065-2776(08)60167-4. [DOI] [PubMed] [Google Scholar]
  23. McDuffie F. C., Brumfield H. W. Effect of rheumatoid factor on complement-mediated phagocytosis. J Clin Invest. 1972 Dec;51(12):3007–3014. doi: 10.1172/JCI107128. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. NISONOFF A., WISSLER F. C., LIPMAN L. N., WOERNLEY D. L. Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bonds. Arch Biochem Biophys. 1960 Aug;89:230–244. doi: 10.1016/0003-9861(60)90049-7. [DOI] [PubMed] [Google Scholar]
  25. PORTER R. R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. doi: 10.1042/bj0730119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Pope R. M., McDuffy S. J. IgG rheumatoid factor. Relationship to seropositive rheumatoid arthritis and absence in seronegative disorders. Arthritis Rheum. 1979 Sep;22(9):988–998. doi: 10.1002/art.1780220907. [DOI] [PubMed] [Google Scholar]
  27. Schmid F. R., Roitt I. M., Rocha M. J. Complement fixation by a two-component antibody system: immunoglobulin G and immunoglobulin M anti-globulin (rheumatoid factor). Parodoxical effect related to immunoglobulin G concentration. J Exp Med. 1970 Oct 1;132(4):673–693. doi: 10.1084/jem.132.4.673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Shivers J. C., Daniels C. A. Effect of rheumatoid factor and anti-immunoglobulin G antibodies on complement-mediated lysis of herpes simplex virus-infected human fibroblasts. Infect Immun. 1977 Feb;15(2):478–484. doi: 10.1128/iai.15.2.478-484.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Tanimoto K., Cooper N. R., Johnson J. S., Vaughan J. H. Complement fixation by rheumatoid factor. J Clin Invest. 1975 Mar;55(3):437–445. doi: 10.1172/JCI107949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Taylor-Upsahl M. M., Abrahamsen T. G., Natvig J. B. Rheumatoid factor plaque-forming cells in rheumatoid synovial tissue. Clin Exp Immunol. 1977 May;28(2):197–203. [PMC free article] [PubMed] [Google Scholar]
  31. Taylor-Upsahl M. M., Johnson P. M., Mellbye O. J., Natvig J. B. A study of complement fixation by rheumatoid factor using a haemolytic assay system. Clin Exp Immunol. 1977 May;28(2):204–211. [PMC free article] [PubMed] [Google Scholar]
  32. Vaughan J. H., Chihara T., Moore T. L., Robbins D. L., Tanimoto K., Johnson J. S., McMillan R. Rheumatoid factor-producing cells detected by direct hemolytic plaque assay. J Clin Invest. 1976 Oct;58(4):933–941. doi: 10.1172/JCI108546. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. WASSERMAN E., LEVINE L. Quantitative micro-complement fixation and its use in the study of antigenic structure by specific antigen-antibody inhibition. J Immunol. 1961 Sep;87:290–295. [PubMed] [Google Scholar]
  34. WILLIAMS R. C., Jr, KUNKEL H. G. Rheumatoid factor, complement, and conglutinin aberrations in patients with subacute bacterial endocarditis. J Clin Invest. 1962 Mar;41:666–675. doi: 10.1172/JCI104523. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Williams R. C., Jr, Mellbye O. J., Kronvall G. Anti-gamma globulins and chronic infection: comparative studies of the immune response to various bacteria and gamma globulin preparations. Infect Immun. 1972 Sep;6(3):316–323. doi: 10.1128/iai.6.3.316-323.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES