Analysis of Foot-and-Mouth Disease Virus Type O Brugge Neutralization Epitopes Using Monoclonal Antibodies Free

Abstract

Summary

Monoclonal antibodies (MAbs) were elicited with inactivated, purified foot-and-mouth disease virus (FMDV) type O strain Brugge (140S) and with 12S protein subunits. Each MAb was tested for its capacity to bind to FMDV O Brugge 140S virions, 12S subunits and purified VP1 by radioimmunoassay (RIA) and to neutralize viral infectivity in mouse protection assays. Those MAbs which reacted only with 12S subunits in RIA did not neutralize infectious virus. One MAb, 12FE9.2.1, reacted with 140S, 12S and purified VP1 of FMDV O Brugge and neutralized infectious virus. Reactions with different biosynthetic FMDV type O Campos VP1 polypeptides localized the binding site of 12FE9.2.1 between amino acid residues 135 and 172. Eight MAbs reacted with both 140S virions and 12S subunits and neutralized infectious virus. Monoclonal antibodies that reacted only with 12S protein subunits or with 140S, 12S and VP1 did not compete in RIA with 140S/12S-reactive neutralizing MAbs for 12S binding sites. The ability of 140S/12S-reactive MAbs to compete for the 12S binding site defined by MAb 10GA4.2.2 was directly related to their capacity to neutralize infectious virus, suggesting that these MAbs were all affecting a single neutralization site. In mouse protection and plaque reduction neutralization assays, 10GA4.2.2 and 12FE9.2.1 were equally effective in neutralizing the homologous FMDV type O Brugge, and in cross-neutralization assays both exhibited high titres against four additional strains of type O FMDV.

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1986-10-01
2024-03-28
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References

  1. Bachrach H. L. 1977; Foot-and-mouth disease virus: properties, molecular biology, and immunogenicity. In Beltsville Symposia in Agricultural Research. I. Virology in Agriculture pp 3–22 Edited by Romberger J. A. Montclair, N.J.: Allanheld, Osmun & Co;
    [Google Scholar]
  2. Bachrach H. L., Trautman R., Breese S. S. 1964; Chemical and physical properties of virtually pure foot-and-mouth disease virus. American Journal of Veterinary Research 25:333–342
    [Google Scholar]
  3. Bachrach H. L., Moore D. M., Mckercher P. D., Polatnick J. 1975; Immune and antibody response to isolated capsid protein of foot-and-mouth disease virus. Journal of Immunology 115:1636–1641
    [Google Scholar]
  4. Bachrach H. L., Moore D. M., Mckercher P. D., Polatnick J. 1977; An experimental subunit vaccine for foot-and-mouth disease. Developments in Biological Standardization 35:155–160
    [Google Scholar]
  5. Bachrach H. L., Morgan D. O., Moore D. M. 1979; Foot-and-mouth disease virus immunogenic capsid protein VPT: N-terminal sequences and immunogenic peptides obtained by CNBr and tryptic cleavages. Intervirology 12:65–72
    [Google Scholar]
  6. Bahnemann H. G. 1975; Binary ethylenimine as an inactivant for foot-and-mouth disease virus and its application for vaccine production. Archives of Virology 47:47–54
    [Google Scholar]
  7. Baxt B., Morgan D. O., Robertson B. H., Timpone C. A. 1984; Epitopes on foot-and-mouth disease virus outer capsid protein VP1 involved in neutralization and cell attachment. Journal of Virology 51:298–305
    [Google Scholar]
  8. Bernard S., Wantyghem J., Grosclaude J., Laporte J. 1974; Chromatographic preparation of purified structural proteins from foot-and-mouth disease virus. Biochemical and Biophysical Research Communications 58:624–632
    [Google Scholar]
  9. Bittle J. L., Houghten R. A., Alexander H., Shinnick T. M., Sutcliffe J. G., Lerner R. A., Rowlands D. J., Brown F. 1982; Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature, London 298:30–33
    [Google Scholar]
  10. Brown F., Smale C. J. 1970; Demonstration of three specific sites on the surface of foot-and-mouth disease virus by antibody complexing. Journal of General Virology 1:115–127
    [Google Scholar]
  11. Cowan K. M. 1968; Immunochemical studies of foot-and-mouth disease. IV. Preparation and evaluation of antisera specific for virus, virus protein subunit and the infection-associated antigen. Journal of Immunology 101:1183–1191
    [Google Scholar]
  12. Dimarchi R., Brooke G., Gale C., Cracknell V., Doel T., Mowat N. 1986; Protection of cattle against foot-and-mouth disease by a synthetic peptide. Science 232:639–641
    [Google Scholar]
  13. Finney D. J. 1964 Statistical Methods in Biological Assay, 2nd edn.. p 571 New York: Hafner Publishing Co;
    [Google Scholar]
  14. Goding J. W. 1983; Monoclonal Antibodies. Principles and Practice London: Academic Press;
    [Google Scholar]
  15. Hardy M. M., Moore D. M. 1981; Neutralization of foot-and-mouth disease virus. I. Sensitization of the 140S virion by antibody also reactive with the 12S protein subunit. Journal of General Virology 55:415–427
    [Google Scholar]
  16. Haresnape J. M., Mccahon D. 1983; Four independent antigenic determinants on the capsid polypeptides of aphthovirus. Journal of General Virology 64:2345–2355
    [Google Scholar]
  17. Kaaden O. R., Adam K.-H., Strohmaier K. 1977; Induction of neutralizing antibodies and immunity in vaccinated guinea pigs by cyanogen bromide-peptides of VP3 of foot-and-mouth disease virus. Journal of General Virology 34:397–400
    [Google Scholar]
  18. Kleid D. G., Yansura D., Small B., Dowbenko D., Moore D. M., Grubman M. J., Mckercher P. D., Morgan D. O., Robertson B. H., Bachrach H. L. 1981; Cloned viral protein vaccine for foot-and-mouth disease: responses in cattle and swine. Science 214:1125–1129
    [Google Scholar]
  19. Kleid D. G., Dowbenko D. J., Bock L. A., Hoatlin M. E., Jackson M. L., Patzer E. J., Shire S. J., Weddell G. N., Yansura D. G., Morgan D. O., Mckercher P. D., Moore D. M. 1985; Production of recombinant vaccines from microorganisms: vaccine for foot-and-mouth disease virus. In Microbiology – 1985 pp 405–408 Edited by Leive L. Washington, D.C.: American Society for Microbiology;
    [Google Scholar]
  20. Köhler G., Milstein C. 1975; Continuous cultures of fused cells secreting antibody of predefined specificity. Nature, London 256:495–497
    [Google Scholar]
  21. Kurz C., Forss S., Kupper H., Strohmaier K., Schaller H. 1981; Nucleotide sequence and corresponding amino-acid sequence of the gene for the major antigen of foot-and-mouth disease virus. Nucleic Acids Research 9:1919–1931
    [Google Scholar]
  22. Laporte J., Grosclaude J., Wantyghem J., Bernard S., Rouze P. 1973; Neutralisation en culture cellulaire du pouvoir infectieux du virus de la fièvre aphteuse par des serums provenant de pores immunisés a l’aide d’une proteine virale purifiée. Comptes rendus hebdomadaires des seances de I’Academie des sciences, série D 276:3399–3402
    [Google Scholar]
  23. Letchworth G. J., Appleton J. A. 1984; Methods for the Production of Monoclonal Antibodies. U. S. Department of Agriculture, Agriculture Handbook No. 630
    [Google Scholar]
  24. Mccullough K. C., Butcher R. 1982; Monoclonal antibodies against foot-and-mouth disease virus 146S and 12S particles. Archives of Virology 74:1–9
    [Google Scholar]
  25. Mckercher P. D., Moore D. M., Morgan D. O., Robertson B. J., Callis J. J., Kleid D. G., Shire S. J., Yansura D. G., Dowbenko D., Small B. 1985; Dose-response evaluation of a genetically engineered foot-and-mouth disease virus polypeptide immunogen in cattle. American Journal of Veterinary Research 46:587–590
    [Google Scholar]
  26. Makoff A. J., Paynter C. A., Rowlands D. J., Boothroyd J. C. 1982; Comparison of the amino acid sequence of the major immunogen from three serotypes of foot and mouth disease virus. Nucleic Acids Research 10:8285–8295
    [Google Scholar]
  27. Meloen R. H., Briaire J., Woortmeyer R. J., Van Zaane D. 1983; The main antigenic determinant detected by neutralizing monoclonal antibodies on the intact foot-and-mouth disease virus particle is absent from isolated VP1. Journal of General Virology 64:1193–1198
    [Google Scholar]
  28. Morgan D. O., Moore D. M., Mckercher P. D. 1980; Vaccination against foot-and-mouth disease. In New Developments with Human and Veterinary Vaccines pp 169–178 Edited by Mizrahi A., Hertman I., Klingberg M. A., Kohn A. New York: Alan R. Liss;
    [Google Scholar]
  29. Morgan D. O., Robertson B. H., Moore D. M., Timpone C. A., Mckercher P. D. 1984; Aphthoviruses: control of foot-and-mouth disease with genetic engineering vaccines. In Control of Virus Diseases pp 135–145 Edited by Kurstak E., Marusyk R. G. New York: Marcel Dekker;
    [Google Scholar]
  30. Ouldridge E. J., Barnett P. V., Parry N. R., Syred A., Head M., Rweyemamu M. M. 1984; Demonstration of neutralizing and non-neutralizing epitopes on the trypsin-sensitive site of foot-and-mouth disease virus. Journal of General Virology 65:203–207
    [Google Scholar]
  31. Pfaff E., Mussgay M., Bohm H. O., Schulz G. E., Schaller H. 1982; Antibodies against a preselected peptide recognize and neutralize foot-and-mouth disease virus. EMBO Journal 1:869–874
    [Google Scholar]
  32. Polatnick J., Bachrach H. L. 1977; Growth of BHK cells for the production and purification of foot-and-mouth disease virus. In Cell Culture and Its Applications pp 603–615 Edited by Acton R. T. New York: Academic Press;
    [Google Scholar]
  33. Robertson B. H., Moore D. M., Grubman M. J., Kleid D. G. 1983; Identification of an exposed region of the immunogenic capsid polypeptide VP1 on foot-and-mouth disease virus. Journal of Virology 46:311–316
    [Google Scholar]
  34. Robertson B. H., Morgan D. O., Moore D. M. 1984; Location of neutralizing epitopes defined by monoclonal antibodies generated against the outer capsid polypeptide, VP1, of foot-and-mouth disease virus A12. Virus Research 1:489–500
    [Google Scholar]
  35. Strohmaier K., Franze R., Adam K.-h. 1982; Location and characterization of the antigenic portion of the FMDV immunizing protein. Journal of General Virology 59:295–306
    [Google Scholar]
  36. Swaney L. M., Bishop F. K., House C. A. 1982; A new continuous bovine kidney cell line susceptible to foot-and-mouth disease virus. Abstracts, Annual Meeting of the American Society for Microbiology p 256 Washington, D.C.: American Society for Microbiology;
    [Google Scholar]
  37. Vande Woude G. F., Swaney J. B., Bachrach H. L. 1972; Chemical and physical properties of foot-and-mouth disease virus: a comparison with Maus-Elberfeld virus. Biochemical and Biophysical Research Communications 48:1222–1229
    [Google Scholar]
  38. Wagner G. G., Card J. L., Cowan K. M. 1970; Immunochemical studies of foot-and-mouth disease. VII. Characterization of foot-and-mouth disease virus concentrated by polyethylene glycol precipitation. Archiv fur die gesamte Virusforschung 30:343–352
    [Google Scholar]
  39. Yansura D. G., Dowbenko D., Weddell G. N., Hoatlin M. E., Shire S. J., Bock L. A., Patzer E. J., Kleid D. G., Moore D. M., Robertson B. H., Grubman M. J., Morgan D. O., Mckercher P. D. 1983; Biosynthetic vaccine for foot-and-mouth disease. In Advances in Gene Technology: Molecular Genetics of Plants and Animals pp 479–493 Edited by Downey K., Voellmy R. W., Ahmad F., Schultz J., Black S. London: Academic Press;
    [Google Scholar]
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