1887

Abstract

Summary

Seven neutralizing monoclonal antibodies were used to characterize 30 escape mutants of a type O foot-and-mouth disease (FMD) virus (O Kaufbeuren) selected with the five most active antibodies. Three non-overlapping antigenic sites were found by ELISA and cross-neutralization studies. Within two of the sites the epitopes of two or more monoclonal antibodies overlapped. Two of the sites were conformation- dependent and could not be detected on virus subunits or isolated denatured polypeptides. The third site was less conformation-dependent since the appropriate monoclonal antibodies were able to bind to 12S subunits, isolated VP1 protein and a synthetic peptide containing residues 141 to 160 of VP1 in ELISA. Electrofocusing of mutants of that site showed a high frequency of electrophoretic alterations in VP1. The sequence of most or all of the VP1 coding region of 10 escape mutants of that site plus three parental isolates was determined by primer extension sequencing. At least five amino acids were found to be involved but in only one case (residue 148 of VP1) did a change at that residue produce complete resistance to neutralization. Partial resistance was produced by changes at residues 144,154 or 208 of VP1 or another residue(s), as yet undefined, that is probably in one of the other capsid polypeptides. Thus the site defined by these mutants was made up of at least three regions, the region involving residues 144 to 154 of VP1, the region encompassing residue 208 from the COOH terminus of VP 1, plus a region, probably of VP2 or VP3, encompassing the undefined residue(s).

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-68-6-1637
1987-06-01
2024-10-08
Loading full text...

Full text loading...

/deliver/fulltext/jgv/68/6/JV0680061637.html?itemId=/content/journal/jgv/10.1099/0022-1317-68-6-1637&mimeType=html&fmt=ahah

References

  1. 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 immunisation with a chemically synthesised peptide predicted from the viral nucleotide sequence. Nature; London: 29830–33
    [Google Scholar]
  2. Brocchi E., Civardi A., De Dimone F., Panina G. F. 1983; Characterisation of foot-and-mouth disease virus antibodies. 20th Congress of the Italian Society of Microbiology, Gardone, Italy. Atti dell Societa italiana delle scienze veterinarie 36:576–578
    [Google Scholar]
  3. Cheung A., Dehamarter J., Weiss S., Kupper H. 1983; Comparison of the major antigen determinants of different serotypes of foot-and-mouth disease virus. Journal of Virology 48:451–459
    [Google Scholar]
  4. Crowther J. R., Mccullough K. C., De Simone F., Brocchi E. 1984; Monoclonal antibodies against FMDV: applications and potential use. Report to the Research Group of the Standing Technical Committee of the European Commission for the Control of FMD (Brescia, Italy) pp 40–51 Rome: F.A.O.;
    [Google Scholar]
  5. De Simone F., Brocchi E., Capucci L., Panina G. F. 1983; Characterisation of monoclonal antibodies to FMD virus. Report to the Research Group of the Standing Technical Committee of the European Commission for the Control of FMD (Brescia, Italy) pp. 17–19 Rome: F.A.O.;
    [Google Scholar]
  6. Di Marchi R., Brooke G., Gale C., Cracknell V., Doel T., Mowat N. 1986; Protection of cattle against foot- and-mouth disease by synthetic peptide. Science 232:639–641
    [Google Scholar]
  7. Forss S., Strebel K., Beck E., Schaller H. 1984; Nucleotide sequence and genome organisation of foot-and- mouth disease virus. Nucleic Acids Research 16:6587–6601
    [Google Scholar]
  8. Geysen A. M., Meloen R. H., Barteling S. J. 1984; Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proceedings of the National Academy of Sciences U.S.A.: 813998–4002
    [Google Scholar]
  9. Geysen A. M., Barteling S. J., Meloen R. H. 1985; Small peptides induce antibodies with a sequence and structural requirement for binding antigen comparable to antibodies raised against the native protein. Proceedings of the National Academy of Sciences U.S.A.: 82178–182
    [Google Scholar]
  10. 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]
  11. Hogle J. M., Chow M., Filman D. J. 1985; The three dimensional structure of poliovirus at 29 A resolution. Science 229:1358–1365
    [Google Scholar]
  12. King A. M. Q., Mccahon D., Slade W. R., Newman J. W. I. 1982; Biochemical evidence of recombination within the unsegmented RNA genome of aphthovirus. Journal of Virology 41:66–77
    [Google Scholar]
  13. La Torre J. L., Underwood B. O., Lebendiker M., Gorman B. M., Brown F. 1982; Application of RNaseT, one- and two-dimensional analyses to the rapid identification of foot-and-mouth disease viruses. Infection and Immunity 36:142–147
    [Google Scholar]
  14. Mccahon D., Slade W. R. 1981; A sensitive method for the detection and isolation of recombinants of foot-and- mouth disease virus. Journal of General Virology 53:333–342
    [Google Scholar]
  15. Mccahon D., King A. M. Q., Roe D. S., Slade W. R., Newman J. W. I., Cleary A. M. 1985; Isolation and biochemical characterisation of intertypic recombinants of foot-and-mouth disease virus. Virus Research 3:87–100
    [Google Scholar]
  16. Mccullough K. C., Crowther J. R., Butcher R. N. 1985; Alteration in antibody reactivity with foot-and- mouth disease virus 146S antigen before and after binding to a solid phase or complexing with specific antibody. Journal of Immunological Methods 82:91–100
    [Google Scholar]
  17. Mccullough K. C., Crowther J. R., Carpenter W. C., Brocchi E., Capucci L., Desimone F., Xie Q., Mccahon D. 1987; Epitopes on foot-and-mouth disease virus particles. I. Topology. Virology in press
    [Google Scholar]
  18. Minor P. D., Ferguson M., Evans D. M. A., Almond J. W., Icenogle J. P. 1986; Antigenic structure of polioviruses of serotypes 1, 2 and 3. Journal of General Virology 67:1283–1291
    [Google Scholar]
  19. Palmenberg A. C., Kirby E. M., Janda M. R., Drake N. L., Duke G. M., Potratz K. F., Collett M. S. 1984; The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region. Nucleic Acids Research 12:2969–2985
    [Google Scholar]
  20. Pfaff E., Mussgay M., Bohm H. O., Shulz G. E., Schaller H. 1982; Antibodies against a preselected peptide recognise and neutralise foot-and-mouth disease virus. EMBO Journal 1:869–874
    [Google Scholar]
  21. Rossmann M. G., Arnold E., Erikson J. W., Frankberger E. A., Griffith J. P., Hecht H.-J., Johnson J. E., Kamer G., Luo M., Mosser A. G., Rueckert R. R., Sherry B., Vriend G. 1985; Structure of a human common cold virus and functional relationship to other picomaviruses. Nature; London: 317145–153
    [Google Scholar]
  22. Rowlands D. J., Clarke B. E., Carroll A. R., Brown F., Nicholson B. H., Bittle J. L., Houghton R. A., Lerner R. A. 1983; Chemical basis of antigenic variation in foot-and-mouth disease virus. Nature; London: 306694–697
    [Google Scholar]
  23. Sherry B., Mosser A. G., Colonna R. J., Rueckert R. R. 1986; Use of monoclonal antibodies to identify four neutralisation immunogens on a common cold picomavirus, human rhinovirus 14. Journal of Virology 51:246–257
    [Google Scholar]
  24. Snowdon W. A. 1966; Growth of FMDV in monolayer cultures of calf thyroid cells. Nature; London: 2101079–1080
    [Google Scholar]
  25. 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]
  26. Webster R. G., Laver W. G., Air G. M. 1983; Antigenic variation among type A influenza viruses. In Genetics of Influenza Viruses pp 127–168 Palese P., Kingsbury D. W. Edited by New York: Springer-Verlag;
    [Google Scholar]
  27. Zimmern D., Kaesberg P. 1978; 3′-Terminal nucleotide sequence of encephalomyocarditis virus RNA determined by reverse transcriptase and chain-terminating inhibitors. Proceedings of the National Academy of Sciences U.S.A.: 754257–4261
    [Google Scholar]
/content/journal/jgv/10.1099/0022-1317-68-6-1637
Loading
/content/journal/jgv/10.1099/0022-1317-68-6-1637
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error