Skip to main content
NCBI home page
Infection and Immunity logoLink to Infection and Immunity
. 1983 Apr;40(1):257–264. doi: 10.1128/iai.40.1.257-264.1983

Importance of complement source in bactericidal activity of human antibody and murine monoclonal antibody to meningococcal group B polysaccharide.

W D Zollinger, R E Mandrell
PMCID: PMC264843  PMID: 6403466

Abstract

The bactericidal activity of human antibody and murine monoclonal antibody to meningococcal group B polysaccharide was investigated as a function of the complement source. The immunoglobulin M murine monoclonal antibody 2-2-B was shown by several different methods to be highly specific for meningococcal group B and Escherichia coli K1 capsular polysaccharides. It had strong bactericidal activity in conjunction with either rabbit or human complement, but gave a higher titer with rabbit complement. A strong prozone was observed in each case. Human postvaccination antibody to meningococcal group B polysaccharide was strongly bactericidal with rabbit complement, but had little or no bactericidal activity in conjunction with human complement. Antibodies in adult normal human sera that were bactericidal with rabbit complement were also found to be predominantly directed against the meningococcal group B capsular polysaccharide. Human antibodies that were bactericidal with human complement appeared to be primarily directed against noncapsular antigens.

Full text

PDF
257

Selected References

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

  1. Akiyama Y., Inoue K. Isolation and properties of complement-resistant strains of Escherichia coli K-12. Infect Immun. 1977 Nov;18(2):446–453. doi: 10.1128/iai.18.2.446-453.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Craven D. E., Shen K. T., Frasch C. E. Natural bactericidal activity of human serum against Neisseria meningitidis isolates of different serogroups and serotypes. Infect Immun. 1982 Jul;37(1):132–137. doi: 10.1128/iai.37.1.132-137.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cross A. S., Zollinger W., Mandrell R., Gemski P., Sadoff J. Evaluation of immunotherapeutic approaches for the potential treatment of infections caused by K1-positive Escherichia coli. J Infect Dis. 1983 Jan;147(1):68–76. doi: 10.1093/infdis/147.1.68. [DOI] [PubMed] [Google Scholar]
  4. Cunniff R. V., Cole H. H., Stollar B. D. Properties of 19S antibodies in complement fixation. II. Selective inactivation of a complement-fixing site by urea. J Immunol. 1968 Oct;101(4):695–701. [PubMed] [Google Scholar]
  5. Deutsch G., Amiraian K. A study of the complement fixing properties of equine antisera. Immunology. 1968 Nov;15(5):623–632. [PMC free article] [PubMed] [Google Scholar]
  6. Frasch C. E., Chapman S. S. Classification of Neisseria meningitidis group B into distinct serotypes. I. Serological typing by a microbactericidal method. Infect Immun. 1972 Jan;5(1):98–102. doi: 10.1128/iai.5.1.98-102.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Frasch C. E. Role of protein serotype antigens in protection against disease due to Neisseria meningitidis. J Infect Dis. 1977 Aug;136 (Suppl):S84–S90. doi: 10.1093/infdis/136.supplement.s84. [DOI] [PubMed] [Google Scholar]
  8. Goldschneider I., Gotschlich E. C., Artenstein M. S. Human immunity to the meningococcus. I. The role of humoral antibodies. J Exp Med. 1969 Jun 1;129(6):1307–1326. doi: 10.1084/jem.129.6.1307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Goldschneider I., Gotschlich E. C., Artenstein M. S. Human immunity to the meningococcus. II. Development of natural immunity. J Exp Med. 1969 Jun 1;129(6):1327–1348. doi: 10.1084/jem.129.6.1327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gray B. M. ELISA methodology for polysaccharide antigens: protein coupling of polysaccharides for adsorption to plastic tubes. J Immunol Methods. 1979;28(1-2):187–192. doi: 10.1016/0022-1759(79)90340-5. [DOI] [PubMed] [Google Scholar]
  11. Griffiss J. M., Bertram M. A. Immunoepidemiology of meningococcal disease in military recruits. II. Blocking of serum bactericidal activity by circulating IgA early in the course of invasive disease. J Infect Dis. 1977 Dec;136(6):733–739. doi: 10.1093/infdis/136.6.733. [DOI] [PubMed] [Google Scholar]
  12. Helting T. B., Guthöhrlein G., Blackkolb F., Ronneberger H. Serotype determinant protein of Neisseria Meningitidis. Large scale preparation by direct detergent treatment of the bacterial cells. Acta Pathol Microbiol Scand C. 1981 Apr;89(2):69–78. [PubMed] [Google Scholar]
  13. Humphires G. M., McConnell H. M. Antigen mobility in membranes and complement-medical immune attack. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2483–2487. doi: 10.1073/pnas.72.7.2483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hänsch G. M., Hammer C. H., Vanguri P., Shin M. L. Homologous species restriction in lysis of erythrocytes by terminal complement proteins. Proc Natl Acad Sci U S A. 1981 Aug;78(8):5118–5121. doi: 10.1073/pnas.78.8.5118. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Jones D. M., Eldridge J. Development of antibodies to meningococcal protein and lipopolysaccharide serotype antigens in healthy-carriers. J Med Microbiol. 1979 Feb;12(1):107–111. doi: 10.1099/00222615-12-1-107. [DOI] [PubMed] [Google Scholar]
  16. Kasper D. L., Winkelhake J. L., Brandt B. L., Artenstein M. S. Antigenic specificity of bactericidal antibodies in antisera to Neisseria meningitidis. J Infect Dis. 1973 Apr;127(4):378–387. doi: 10.1093/infdis/127.4.378. [DOI] [PubMed] [Google Scholar]
  17. Kasper D. L., Wyle F. A., Formal S. B. Bactericidal antibody assay using 14 C-labeled Neisseria meningitidis. Proc Soc Exp Biol Med. 1972 Apr;139(4):1175–1180. doi: 10.3181/00379727-139-36324. [DOI] [PubMed] [Google Scholar]
  18. Kearney J. F., Radbruch A., Liesegang B., Rajewsky K. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J Immunol. 1979 Oct;123(4):1548–1550. [PubMed] [Google Scholar]
  19. Kennett R. H. Cell fusion. Methods Enzymol. 1979;58:345–359. doi: 10.1016/s0076-6879(79)58149-x. [DOI] [PubMed] [Google Scholar]
  20. Lim D., Gewurz A., Lint T. F., Ghaze M., Sepheri B., Gewurz H. Absence of the sixth component of complement in a patient with repeated episodes of meningococcal meningitis. J Pediatr. 1976 Jul;89(1):42–47. doi: 10.1016/s0022-3476(76)80924-9. [DOI] [PubMed] [Google Scholar]
  21. Mandrell R. E., Zollinger W. D. Measurement of antibodies to meningococcal group B polysaccharide: low avidity binding and equilibrium binding constants. J Immunol. 1982 Nov;129(5):2172–2178. [PubMed] [Google Scholar]
  22. Moll A., Manning P. A., Timmis K. N. Plasmid-determined resistance to serum bactericidal activity: a major outer membrane protein, the traT gene product, is responsible for plasmid-specified serum resistance in Escherichia coli. Infect Immun. 1980 May;28(2):359–367. doi: 10.1128/iai.28.2.359-367.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Peter G., Weigert M. B., Bissel A. R., Gold R., Kreutzer D., McLean R. H. Meningococcal meningitis in familial deficiency of the fifth component of complement. Pediatrics. 1981 Jun;67(6):882–886. [PubMed] [Google Scholar]
  24. Reller L. B., MacGregor R. R., Beaty H. N. Bactericidal antibody after colonization with Neisseria meningitidis. J Infect Dis. 1973 Jan;127(1):56–62. doi: 10.1093/infdis/127.1.56. [DOI] [PubMed] [Google Scholar]
  25. Stollar B. D., Stadecker M. J., Morecki S. Comparison of the inactivation of IgM and IgG complement fixation sites by acid and base. J Immunol. 1976 Oct;117(4):1387–1391. [PubMed] [Google Scholar]
  26. Tee G. L., Scott G. K. Analysis of outer membrane components of Escherichia coli ML308 225 and of a serum-resistant mutant. Infect Immun. 1980 May;28(2):387–392. doi: 10.1128/iai.28.2.387-392.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Tettmar R. E., Abbott J. D., Jones D. M. Meningococcal meningitis in Royal Air Force recruits. Public Health. 1977 Sep;91(5):253–257. doi: 10.1016/s0033-3506(77)80054-1. [DOI] [PubMed] [Google Scholar]
  28. Wong K. H., Barrera O., Sutton A., May J., Hochstein D. H., Robbins J. D., Robbins J. B., Parkman P. D., Seligmann E. B., Jr Standardization and control of meningococcal vaccines, group A and group C polysaccharides. J Biol Stand. 1977;5(3):197–215. doi: 10.1016/s0092-1157(77)80005-x. [DOI] [PubMed] [Google Scholar]
  29. Wyle F. A., Artenstein M. S., Brandt B. L., Tramont E. C., Kasper D. L., Altieri P. L., Berman S. L., Lowenthal J. P. Immunologic response of man to group B meningococcal polysaccharide vaccines. J Infect Dis. 1972 Nov;126(5):514–521. doi: 10.1093/infdis/126.5.514. [DOI] [PubMed] [Google Scholar]
  30. Zollinger W. D., Dalrymple J. M., Artenstein M. S. Analysis of parameters affecting the solid phase radioimmunoassay quantitation of antibody to meningococcal antigens. J Immunol. 1976 Nov;117(5 PT2):1788–1798. [PubMed] [Google Scholar]
  31. Zollinger W. D., Mandrell R. E., Altieri P., Berman S., Lowenthal J., Artenstein M. S. Safety and immunogenicity of a Neisseria meningitidis type 2 protein vaccine in animals and humans. J Infect Dis. 1978 Jun;137(6):728–739. doi: 10.1093/infdis/137.6.728. [DOI] [PubMed] [Google Scholar]
  32. Zollinger W. D., Mandrell R. E., Griffiss J. M., Altieri P., Berman S. Complex of meningococcal group B polysaccharide and type 2 outer membrane protein immunogenic in man. J Clin Invest. 1979 May;63(5):836–848. doi: 10.1172/JCI109383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Zollinger W. D., Mandrell R. E. Outer-membrane protein and lipopolysaccharide serotyping of Neisseria meningitidis by inhibition of a solid-phase radioimmunoassay. Infect Immun. 1977 Nov;18(2):424–433. doi: 10.1128/iai.18.2.424-433.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES