1887

Abstract

The binding capacity and the protective activity of three monoclonal antibodies (MAbs) – ARM 1-4, ARM 1-7 and ARM 2-2 – obtained from spleen cells of mice immunised with O6:K– pre-treated with sub-MIC of aztreonam were studied. The MAbs belonged to IgG isotype and showed different reactivity toward protein epitopes of in an immunoblotting assay. ARM 1-4 recognised epitopes on molecules of 30 kDa and 40 kDa. ARM 1-7 identified an epitope of a molecule of 41 kDa, and ARM 2-2 recognised epitopes of molecules of 15 kDa and 41 kDa. In ELISA the MAbs cross-reacted with O7:K–, O111:B4 and O128:K– with different binding affinity. Furthermore, the MAbs showed complement-dependent bactericidal activity. The MAbs displayed different protective capacities when given to mice 90 min before lethal challenges with 2 × LD50, 4 × LD50 and 8 × LD50 of strains. In all but one instance (ARM 1-4 O7:K–) it was not possible to correlate protective capacity with binding affinity of a MAb to a given bacterial cell. Therefore, the epitopes recognised by the MAb may be more closely associated with bacterial virulence than in binding to the bacterial cell.

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1997-02-01
2022-01-21
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References

  1. Young L. S., Proctor R. A., Beutler B., McCabe W. R., Sheagren J. N. University of California-Davis interdepartmental conference on gram-negative septicemia. Rev Infect Dis 1991; 13:666–687
    [Google Scholar]
  2. Increase in national hospital discharge survey rates for septicemia United States 1979–1987. MMWR 1990; 39:31–34
    [Google Scholar]
  3. Silva A. T., Bayston K. F., Cohen J. Prophylactic and therapeutic effects of a monoclonal antibody to tumor necrosis factor-α in experimental Gram-negative shock. J Infect Dis 1990; 162:421–427
    [Google Scholar]
  4. Teng N. N. H., Kaplan H. S., Hebert J. M. Protection against Gram-negative bacteremia and endotoxemia with human monoclonal IgM antibodies. Proc Natl Acad Sci USA 1985; 82:1790–1794
    [Google Scholar]
  5. Ziegler E. J., Fischer C. J., Sprung C. L. Treatment of Gram-negative bacteraemia and septic shock with HA-1A human monoclonal antibody against endotoxin. A randomized, doubleblind, placebo-controlled trial. N Engl J Med 1991; 324:429–436
    [Google Scholar]
  6. Baumgartner J.-D., Glauser M. P., McCutchan J. A Prevention of Gram-negative shock and death in surgical patients by antibody to endotoxin core glycolipid. Lancet 1985; 2:59–63
    [Google Scholar]
  7. Nikaido H., Vaara M. Outer membrane. In Neidhardt F. C., Ingraham J. L., Low K. B., Magasanik B., Schaechter M., Umbarger H. E. (eds) Escherichia coli and Salmonella typhimurium Cellular and molecular biology vol 1 Washington, DC: American Society for Microbiology; 19877–22
    [Google Scholar]
  8. Morrin M., Reen D. J. Role of IgG subclass response to outer membrane proteins in inhibiting adhesion of Pseudomonas aeruginosa to epithelial cells. J Med Microbiol 1993; 39:467–472
    [Google Scholar]
  9. Cloeckaert A., Jaques I., Bosseray N. Protection conferred on mice by monoclonal antibodies directed against outer-membrane-protein antigens of Brucella. J Med Microbiol 1991; 34:175–180
    [Google Scholar]
  10. Hamel J., Brodeur B. R., Larose Y., Tsang P. S., Belmaaza A., Montplaisir S. A monoclonal antibody directed against a serotype specific, outer-membrane protein of Haemophilus influenzae type B. J Med Microbiol 1987; 23:163–170
    [Google Scholar]
  11. Goldblatt D., Scadding G. K., Lund V. J., Wade A. M., Turner M. W., Pandey J. P. Association of Gm allotypes with the antibody response to outer membrane proteins of a common upper respiratory tract organism, Moraxella catarrhalis. J Immunol 1994; 153:5316–5320
    [Google Scholar]
  12. Gonzalez C. R., Isibasi A., Ortiz Navarrete V. Lymphocytic proliferative response to outer-membrane proteins isolated from Salmonella. Microbiol Immunol 1993; 37:793–799
    [Google Scholar]
  13. Lun M. T., Amatucci A. M., Raponi G. Murine monoclonal antibody elicited with antibiotic-exposed Escherichia coli exerts protective capacity in experimental bacterial infections. J Med Microbiol 1994; 41:179–183
    [Google Scholar]
  14. Raponi G., Keller N., Overbeek B. P. Immunization of mice with antibiotic-treated Escherichia coli results in enhanced protection against challenge with homologous and heterologous bacteria. J Infect Dis 1991; 163:122–127
    [Google Scholar]
  15. Fazekas De St Groth S., Scheidegger D. Production of monoclonal antibodies: strategy and tactics. J Immunol Methods 1980; 35:1–21
    [Google Scholar]
  16. Brodeur B. R., Tsang P., Larose Y. Parameters affecting ascites tumour formation in mice and monoclonal antibody production. J Immunol Methods 1984; 71:265–272
    [Google Scholar]
  17. Eliasson M., Olsson A., Palmcrantz E. Chimeric IgG-binding receptors engineered from staphylococcal protein A and streptococcal protein G. J Biol Chem 1988; 263:4323–4327
    [Google Scholar]
  18. Overbeek B. P., Schellekens J. F. P., Lippe W., Dekker B. A. T., Verhoef J. Carumonam enhances reactivity of Escherichia coli with mono- and polyclonal antisera to rough mutant Escherichia coli J5. J Clin Microbiol 1987; 25:1009–1013
    [Google Scholar]
  19. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 221:680–685
    [Google Scholar]
  20. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76:4350–4354
    [Google Scholar]
  21. Andrews A. T. Electrophoresis: theory, techniques, and biochemical and clinical applications. 2nd edn. In Peacock A. R., Harrington W. R. (eds) Monographs on physical biochemistry Oxford: Clarendon Press; 1986
    [Google Scholar]
  22. Ziegler E. J., McCutchan J. A., Fierer J. Treatment of Gram-negative bacteremia and shock with human antiserum to a mutant Escherichia coli. N Engl J Med 1982; 307:1225–1230
    [Google Scholar]
  23. Lun M. T., Raponi R., Giordano A. Opsonic activity of intravenous immunoglobulin on Gram-negative bacteria exposed to a monobactam antibiotic. Serodiagn Immunother Infect Dis 1989; 3:241–248
    [Google Scholar]
  24. Leying H., Suerbaum S., Kroll H.-P., Karch H., Opferkuch W. Influence of beta-lactam antibiotics and ciprofloxacin on composition and immunogenicity of Escherichia coli outer membrane. Antimicrob Agents Chemother 1986; 30:475–480
    [Google Scholar]
  25. Overbeek B. P., Veringa E. M. Role of antibodies and antibiotics in aerobic gram-negative septicemia: possible synergism between antimicrobial treatment and immunotherapy. Rev Infect Dis 1991; 13:751–760
    [Google Scholar]
  26. Cevenini R., Sambri V., Massaria F., LaPlaca M., Brocchi E., DeSimone F. Complement-mediated in vitro bactericidal activity of monoclonal antibodies reactive with outer-surface protein OspB of Borrelia burgdorferi. FEMS Microbiol Lett 1992; 90:147–152
    [Google Scholar]
  27. Raponi G., Lun M. T., Lorino G. Reactivity and protective capacity of a polyclonal antiserum derived from mice immunized with antibiotic exposed Escherichia coli. J Antimicrob Chemother 1993; 31:117–128
    [Google Scholar]
  28. Osborn M. J., Wu H. C. P. Proteins of the outer membrane of gram-negative bacteria. Annu Rev Microbiol 1980; 34:369–422
    [Google Scholar]
  29. Kervella M., Fauchère J.-L., Fourel D., Pagès J.-M. Immunological cross-reactivity between outer membrane pore proteins of Campylobacter jejuni and Escherichia coli. FEMS Microbiol Lett 1992; 99:281–286
    [Google Scholar]
  30. Neidhart F. C., VanBogelen R. A. Heat shock response. In Neidhart F. C., Ingraham J. L., Low K. B., Magasanik B., Schaechter M., Umbarger H. E. (eds) Escherichia coli and Salmonella typhimurium. Cellular and molecular biology vol 2 Washington, DC: American Society for Microbiology; 19871334–1345
    [Google Scholar]
  31. Hofstra H., van Tol M. J. D., Dankert J. Cross-reactivity of major outer membrane proteins of Enterobacteriaceae, studied by crossed immunoelectrophoresis. J Bacteriol 1980; 143:328–337
    [Google Scholar]
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