Archives of Virology

, Volume 126, Issue 1, pp 21–33

Characterization of neutralizing antibodies to bovine enterovirus elicited by synthetic peptides

Authors

  • M. S. Smyth
    • Medical Biology Centre, School of Biology and BiochemistryThe Queen's University of Belfast
  • A. Trudgett
    • Medical Biology Centre, School of Biology and BiochemistryThe Queen's University of Belfast
  • E. M. Hoey
    • Medical Biology Centre, School of Biology and BiochemistryThe Queen's University of Belfast
  • S. J. Martin
    • Medical Biology Centre, School of Biology and BiochemistryThe Queen's University of Belfast
  • F. Brown
    • Department of VirologyWellcome Biotechnology Ltd.
Original Papers

DOI: 10.1007/BF01309681

Cite this article as:
Smyth, M.S., Trudgett, A., Hoey, E.M. et al. Archives of Virology (1992) 126: 21. doi:10.1007/BF01309681

Summary

Six synthetic peptides corresponding to regions of bovine enterovirus (BEV), strain VG-5-27, elicited antibodies in mice which reacted with the virus in various assays. These antibodies have been characterised on the basis of their ability to (1) neutralize the virus, (2) bind to the intact virus particle in an immunoprecipitation test, (3) react with the denatured viral proteins, and (4) give immunofluorescent staining of virus infected cells. We have also determined the proportion of antipeptide antibody which binds to the virus in each case. All of the sera immunoprecipitated the virus and neutralized its activty to varying extents. Two of the sera specific for VP 1 sequences failed to react with denatured VP 1 whereas all the other antisera reacted with their respective parental proteins. All of the sera reacted with VG-5-27 infected cells in an immunofluorescence test. The proportion of antibodies to each peptide recognizing intact virus was variable and did not appear to correlate with neutralizing activity. In addition, the ability of each of the sera to react with and neutralize three other strains of the virus was analysed. With one of these strains significant cross-neutralization was observed.

Copyright information

© Springer-Verlag 1992