1887

Abstract

A synthetic peptide vaccine of the general sequence Cys-Cys-(200-213)-Pro-Pro-Ser-(141–158)-Pro-Cys-Gly(peptide A40), where the numbered residues refer to the VP1 sequence of foot-and-mouth disease virus (FMDV) strain A Cruzeiro, has previously been shown to elicit neutralizing and protective antibodies in guinea-pigs and cattle. To examine this immunogenic tract in more detail monoclonal antibodies (MAbs) were raised to this peptide. One such MAb, C1.1, which recognized the homologous peptide, bound to native virus, neutralized infectivity and passively protected mice from challenge. Using overlapping dodecameric peptides the minimum binding ‘footprint’ of this MAb incorporated residues 149–154 which were respectively Gly-Ser-Leu-Ala-Ala-Arg. Since this ‘footprint’ occurs in several other A subtype strains of FMDV, the extent to which MAb C1.1 could cross-react was also examined. Using a liquid-phase competition ELISA, only viruses with a sequence that encompassed the same minimum binding ‘footprint’, namely A Cundinamarca Colombia/76, A Argentina/79, and A Venceslau Brazil/76 reacted with similar affinity against MAb C1.1. However, further serological examination of C1.1 with these viruses by indirect ELISA, neutralization and passive protection showed clear functional disparity. In contrast to the liquid-phase ELISA, the ability of C1.1 to react with electrostatically bound virus varied significantly depending on the subtype examined. Moreover, the capacity of this MAb to neutralize these subtypes showed wide divergence which was mirrored by the protection data.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-77-5-1011
1996-05-01
2022-01-22
Loading full text...

Full text loading...

/deliver/fulltext/jgv/77/5/JV0770051011.html?itemId=/content/journal/jgv/10.1099/0022-1317-77-5-1011&mimeType=html&fmt=ahah

References

  1. Acharya R., Fry E., Stuart D., Fox G., Rowlands D., Brown F. 1989; The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution. Nature 337:709–716
    [Google Scholar]
  2. Al Moudallal Z., Briand J. P., Van Regenmortel M. H. V. 1982; Monoclonal antibodies as probes of the antigenic structure of tobacco mosaic virus. EMBO Journal 1:1005–1010
    [Google Scholar]
  3. Barnett P. V., Rowlands D. J., Parry N. R. 1993; Characterization of monoclonal antibodies raised against a synthetic peptide capable of inducing a neutralizing response to human rhinovirus type 2. Journal of General Virology 74:1295–1302
    [Google Scholar]
  4. Barnett P. V., Rowlands D. J., Campbell R. O., Parry N. R. 1995; Monoclonal antibodies to a peptide of human rhinovirus type 2 with different specificities recognize the same minimum sequence. Journal of General Virology 76:1255–1261
    [Google Scholar]
  5. Beck E., Strohmaier K. 1987; Subtyping of European foot-and-mouth disease virus strains by nucleotide sequence determination. Journal of Virology 61:1621–1629
    [Google Scholar]
  6. 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 298:30–33
    [Google Scholar]
  7. Bolwell C., Clarke B. E., Parry N. R., Ouldridge E. J., Brown F., Rowlands D. J. 1989; Epitope mapping of foot-and-mouth disease virus with neutralizing monoclonal antibodies. Journal of General Virology 70:59–68
    [Google Scholar]
  8. Booth J. C., Rweyemamu M. M., Pay T. W. F. 1978; Dose response relationships in a microneutralization test for foot-and-mouth disease viruses. Journal of Hygiene 80:31–42
    [Google Scholar]
  9. Brioen P., Dekegel D., Boeye A. 1983; Neutralization of poliovirus by antibody-mediated polymerization. Virology 127:463–468
    [Google Scholar]
  10. Brown F., Cartwright B. 1963; Purification of radioactive foot- and-mouth disease virus. Nature 199:1168–1170
    [Google Scholar]
  11. Butcher R. N., Obi T. U., McCullough K. C. 1991; Rapid isolation of monoclonal hybridoma cultures by a ‘fusion-cloning’ method: the requirement for aminopterin. Biologicals 19:171–175
    [Google Scholar]
  12. Cooper H. M., Jemmerson R., Hunt D. F., Griffin P. R., Yates J. R., Shabanowitz J., Zhu N., Paterson Y. 1987; Site-directed chemical modification of horse cytochrome C results in changes in antigenicity due to local and long-range conformational perturbations. Journal of Biological Chemistry 262:11592–11597
    [Google Scholar]
  13. DiMarchi R., Brooke G., Gale C., Cracknell V., Doel T., Mow at N. 1986; Protection of cattle against foot-and-mouth disease by a synthetic peptide. Science 232:639–641
    [Google Scholar]
  14. Doel T. R., Gale C., Do Amaral M. C. F., Mulcahy G., DiMarchi R. 1990; Heterotypic protection induced by synthetic peptides corresponding to three serotypes of foot-and-mouth disease virus. Journal of Virology 64:2260–2264
    [Google Scholar]
  15. Doel T. R., Doel C. M. F. A., Staple R. F., DiMarchi R. 1992; Cross-reactive and serotype-specific antibodies against foot- and-mouth disease virus generated by different regions of the same synthetic peptide. Journal of Virology 66:2187–2194
    [Google Scholar]
  16. Ferguson M., Reed S. E., Minor P. D. 1986; Reactivity of antipeptide and anti-poliovirus type 3 monoclonal antibodies with synthetic peptides. Journal of General Virology 67:2527–2531
    [Google Scholar]
  17. Fox G., Parry N. R., Barnett P. V., McGinn B., Rowlands D. J., Brown F. 1989; The cell attachment site on foot- and-mouth disease virus includes the amino acid sequence RGD (arginineglycine-aspartic acid). Journal of General Virology 70:625–637
    [Google Scholar]
  18. Hastings G. Z., Speller S. A., Francis M. J. 1990; Neutralizing antibodies to human rhinovirus produced in laboratory animals and humans that recognize a linear sequence from VP2. Journal of General Virology 71:3055–3059
    [Google Scholar]
  19. Ibrahimi I. M., Prager E. M., White T. J., Wilson A. C. 1979; Amino acid sequence of California quail lysozyme: effect of evolutionary substitutions on the antigenic structure of lysozyme. Biochemistry 13:2736–2744
    [Google Scholar]
  20. Karber G. 1931; Beitrag zur kollektiven Behandlung pharmako-logischer Reihenversuche. Archiv fur experimentelle Pathologie und Pharmakologie 162:480–483
    [Google Scholar]
  21. McCullough K. C., Crowther J. R., Butcher R. N. 1985; Alteration in antibody reactivity with foot- and-mouth disease virus (FMDV) 146S antigen before and after binding to a solid phase or complexing with specific antibody. Journal of Immunological Methods 82:91–100
    [Google Scholar]
  22. Mason P. W., Reider E., Baxt B. 1994; RGD sequence of foot- and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway. Proceedings of the National Academy of Sciences, USA 91:1932–1936
    [Google Scholar]
  23. Merrifield R. B. 1963; Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. Journal of the American Chemical Society 85:2149–2154
    [Google Scholar]
  24. Mosser A. G., Leippe D. M., Rueckert R. R. 1989; Neutralization of picornaviruses: support for the pentamer bridging hypothesis. In Molecular Aspects of Picornavirus Infection and Detection pp 156–158 Edited by Semler B. L., Ehrenfeld E. Washington, DC: American Society for Microbiology;
    [Google Scholar]
  25. Mulcahy G., Pullen L. A., Gale C., DiMarchi R. D., Doel T. R. 1991; Mouse protection test as a predictor of the protective capacity of synthetic foot-and-mouth disease vaccines. Vaccine 9:19–24
    [Google Scholar]
  26. Parry N. R., Ouldridge E. J., Barnett P. V., Clarke B. E., Francis M. J., Fox J. D., Rowlands D. J., Brown F. 1989; Serological prospects for peptide vaccines against foot-and-mouth disease virus. Journal of General Virology 70:2919–2930
    [Google Scholar]
  27. Parry N., Fox G., Rowlands D., Brown F., Fry E., Acharya R., Logan D., Stuart D. 1990; Structural and serological evidence for a novel mechanism of antigenic variation in foot- and-mouth disease virus. Nature 347:569–572
    [Google Scholar]
  28. Pfaff E., Mussgay M., Bohm H. O., Schulz G. E., Schaller H. 1982; Antibodies against a preselected peptide recognise and neutralize foot- and-mouth disease virus. EMBO Journal 1:869–874
    [Google Scholar]
  29. Rweyemamu M. M., Hingley P. J. 1984; Foot- and-mouth disease virus strain differentiation: analysis of the serological data. Journal of Biological Standardization 12:323–337
    [Google Scholar]
  30. 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]
  31. Thomas A. A. M., Brioen P., Boeye A. 1985; A monoclonal antibody that neutralizes poliovirus by cross-linking virions. Journal of Virology 54:7–13
    [Google Scholar]
  32. Tormo J., Blaas D., Parry N. R., Rowlands D., Stuart D., Fita I. 1994; Crystal structure of a human rhino virus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2. EMBO Journal 13:2247–2256
    [Google Scholar]
  33. Weddell G. N., Yansura D. G., Dowbenko D. J., Hoatlin M. E., Grubman M. J., Moore D. M., Kleid D. G. 1985; Sequence variation in the gene for the immunogenic capsid protein VP1 of foot- and-mouth disease virus type A. Proceedings of the National Academy of Sciences, USA 82:2618–2622
    [Google Scholar]
  34. Wetz K. 1993; Attachment of neutralizing antibodies stabilizes the capsid of poliovirus against uncoating. Virology 192:465–472
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-77-5-1011
Loading
/content/journal/jgv/10.1099/0022-1317-77-5-1011
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

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