1887

Abstract

Summary

The antibody response of cattle to the minor 89-kDa outer-membrane protein (OMP) of brucella was measured by indirect ELISA with the purified protein and compared with the antibody response to smooth lipopolysaccharide (S-LPS). Pre-incubating sera with sonicated cell extracts of prevented the binding of antibodies from uninfected animals to the 89-kDa OMP, suggesting the presence of one or more cross-reactive epitopes on this protein. In cattle infected experimentally with , the antibody response to the 89-kDa OMP was later and less intense than that to S-LPS. In naturally infected cattle, 68% of animals showing an antibody response to S-LPS also showed an antibody response to the 89-kDa OMP. Results indicate that specific epitopes of the 89-kDa OMP in combination with those of other OMPs could be useful for diagnosis of brucellosis in cattle.

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1993-12-01
2024-12-06
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References

  1. Dubray G. Antigens of diagnostic significance in Brucella. In: Verger JM, Plommet M. (eds) Brucella melitensis, a CEE seminar The Hague: Martinus Nijhoff Publishing; 1985123–138
    [Google Scholar]
  2. Cloeckaert A, Jacques I, de Wergifosse P, Dubray G, Limet JN. Protection against Brucella melitensis or Brucella abortus in mice with immunoglobulin G (IgG), IgA, and IgM monoclonal antibodies specific for a common epitope shared by the Brucella A and M smooth lipopolysac- charides. Infect Immun 1992; 60:312–315
    [Google Scholar]
  3. Limet JN, Bosseray N, Garin-Bastuji B, Dubray G, Plommet M. Humoral immunity in mice mediated by monoclonal antibodies against the A and M antigens of Brucella. J Med Microbiol 1989; 30:37–43
    [Google Scholar]
  4. Montaraz JA, Winter AJ, Hunter DM, Sowa BA, Wu AM, Adams LG. Protection against Brucella abortus in mice with O-polysaccharide-specific monoclonal antibodies. Infect Immun 1986; 51:961–963
    [Google Scholar]
  5. Phillips M, Deyoe BL, Canning PC. Protection of mice against Brucella abortus infection by inoculation with monoclonal antibodies recognizing Brucella O-antigen. Am J Vet Res 1989; 50:2158–2161
    [Google Scholar]
  6. Jacques I, Olivier-Bernardin V, Dubray G. Induction of antibody and protective responses in mice by Brucella O-polysaccharide-BSA conjugate. Vaccine 1991; 9:896–900
    [Google Scholar]
  7. Winter AJ, Rowe GE, Duncan JR et al. Effectiveness of the natural and synthetic complexes of porin and O polysaccharide as vaccines against Brucella abortus in mice. Infect Immun 1988; 56:2808–2817
    [Google Scholar]
  8. Cloeckaert A, de Wergifosse P, Dubray G, Limet JN. Identification of seven surface-exposed Brucella outer membrane proteins by use of monoclonal antibodies: immunogold labelling for electron microscopy and enzyme-linked immunosorbent assay. Infect Immun 1990; 58:3980–3987
    [Google Scholar]
  9. Cloeckaert A, Jacques I, Bosseray N et al. 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. Cloeckaert A, Kerkhofs P, Limet JN. Antibody response to Brucella outer membrane proteins in bovine brucellosis: immunoblot analysis and competitive enzyme-linked immunosorbent assay using monoclonal antibodies. J Clin Microbiol 1992; 30:3168–3174
    [Google Scholar]
  11. Dubray G, Charriaut C. Evidence of three major polypeptide species and two major polysaccharide species in the Brucella outer membrane. Ann Rech Vet 1983; 14:311–318
    [Google Scholar]
  12. Douglas JT, Rosenberg EY, Nikaido H, Verstreate DR, Winter AJ. Porins of Brucella species. Infect Immun 1984; 44:16–21
    [Google Scholar]
  13. Verstreate DR, Creasy MT, Caveney NT, Baldwin CL, Blab MW, Winter AJ. Outer membrane proteins of Brucella abortus: isolation and characterization. Infect Immun 1982; 35:979–989
    [Google Scholar]
  14. Cloeckaert A, Zygmunt MS, de Wergifosse P, Dubray G, Limet JN. Demonstration of peptidoglycan-associated Brucella outer-membrane proteins by use of monoclonal antibodies. J Gen Microbiol 1992; 138:1543–1550
    [Google Scholar]
  15. Sowa BA, Kelly KA, Ficht TA, Frey M, Adams LG. SDS-soluble and peptidoglycan-bound proteins in the outer membrane-peptidoglycan complex of Brucella abortus. Vet Microbiol 1991; 27:351–369
    [Google Scholar]
  16. Gomez-Miguel MJ, Moriyon I. Demonstration of a peptido-glycan-linked lipoprotein and characterization of its trypsin fragment in the outer membrane of Brucella spp. Infect Immun 1986; 53:678–684
    [Google Scholar]
  17. Gomez-Miguel MJ, Moriyon I, Alonso-Urmeneta B, Riezu-Boj JI, Diaz R. Serological response to the outer membrane lipoprotein in animal brucellosis. Infect Immun 1988; 56:716–718
    [Google Scholar]
  18. Gomez-Miguel MJ, Moriyon I, Lopez J. Brucella outer membrane lipoprotein shares antigenic determinants with Escherichia coli Braun lipoprotein and is exposed on the cell surface. Infect Immun 1987; 55:258–262
    [Google Scholar]
  19. Leong D, Dfaz R, Milner K, Rudbach J, Wilson JB. Some structural and biological properties of Brucella endotoxin. Infect Immun 1970; 1:174–182
    [Google Scholar]
  20. Lee C, Levin A, Branton D. Copper staining: a five-minute protein stain for sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem 1987; 166:308–312
    [Google Scholar]
  21. Oakley BR, Kirsch DR, Morris NR. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 1980; 105:361–363
    [Google Scholar]
  22. Letesson JJ, Lostrie-Trussart N, Depelchin A. Production d’anticorps monoclonaux specifiques d’isotypes d’imm- unoglobulines. Ann Med Vet 1985; 129:131–141
    [Google Scholar]
  23. Cloeckaert A, Zygmunt MS, Nicolle J-C, Dubray G, Limet JN. O-chain expression in the rough Brucella melitensis strain B115: induction of O-polysaccharide-specific monoclonal antibodies and intracellular localization demonstrated by immunoelectron microscopy. J Gen Microbiol 1992; 138:1211–1219
    [Google Scholar]
  24. Jones LM, Diaz R, Taylor AG. Characterization of allergens prepared from smooth and rough strains of Brucella melitensis. Br J Exp Pathol 1973; 54:492–508
    [Google Scholar]
  25. Zygmunt MS, Gilbert FB, Dubray G. Purification, characterization, and seroreactivity of a 20-Kilodalton Brucella protein antigen. J Clin Microbiol 1992; 30:2662–2667
    [Google Scholar]
  26. Zygmunt MS, Martin J-C, Dubray G. Analysis of immune response: comparison of immunoblots after isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis using cytoplasmic protein extract from Brucella. FEMS Microbiol Lett 1990; 70:263–268
    [Google Scholar]
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