A Conformational Immunogen on VP-2 of Infectious Bursal Disease Virus that Induces Virus-neutralizing Antibodies that Passively Protect Chickens

References

1. Azad A. A., Jagadish M. N., Brown M. A., Hudson P. J. 1987; Deletion mapping and expression in Escherichia coli of the large genomic segment of a birnavirus. Virology 161:145–152
   [Google Scholar]
2. Becht H. 1980; Infectious bursal disease virus. Current Topics in Microbiology and Immunology 90:107–121
   [Google Scholar]
3. Becht H., Müller H., Müller H. K. 1988; Comparative studies on structural and antigenic properties of two serotypes of infectious bursal disease virus. Journal of General Virology 69:631–640
   [Google Scholar]
4. 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]
5. Burnette W. N. 1981; “Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Analytical Biochemistry 112:195–203
   [Google Scholar]
6. Cohen G. H., Dietzschold B., Ponce De Leon M., Long D., Golub E., Varrichio A., Pereira L., Eisenberg R. J. 1984; Localization and synthesis of an antigenic determinant of herpes simplex virus glycoprotein D that stimulates the production of neutralizing antibody. Journal of Virology 49:102–108
   [Google Scholar]
7. Cohen G. H., Isola V. J., Kuhns J., Berman P. W., Eisenberg R. J. 1986; Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: use of a nondenaturing (“native” gel) system of polyacrylamide gel electrophoresis coupled with Western blotting. Journal of Virology 60:157–166
   [Google Scholar]
8. Dobos P. 1979; Peptide map comparison of the proteins of infectious bursal disease virus. Journal of Virology 32:1046–1050
   [Google Scholar]
9. Dyall-Smith M. L., Lazdins I., Tregear G. W., Holmes I. H. 1986; Location of the major antigenic sites involved in rotavirus serotype-specific neutralization. Proceedings of the National Academy of Sciences, U.S.A 83:3465–3468
   [Google Scholar]
10. Fahey K. J., O’donnell I. J., Azad A. A. 1985a; Characterization by Western blotting of the immunogens of infectious bursal disease virus. Journal of General Virology 66:1479–1488
    [Google Scholar]
11. Fahey K. J., O’donnell I. J., Bagust T. J. 1985b; Antibody to the 32K structural protein of infectious bursal disease virus neutralizes viral infectivity in vitro and confers protection on young chickens. Journal of General Virology 66:2693–2702
    [Google Scholar]
12. Hudson P. J., Mckern N. M., Power B. E., Azad A. A. 1986; Genomic structure of the large RNA segment of infectious bursal disease virus. Nucleic Acids Research 14:5001–5012
    [Google Scholar]
13. Jiménez G., Correa I., Melgosa M. P., Bullido M. J., Enjuanes L. 1986; Critical epitopes in transmissible gastroenteritis virus neutralization. Journal of Virology 60:131–139
    [Google Scholar]
14. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 111:680–685
    [Google Scholar]
15. Lerner R. A. 1982; Tapping of the immunological repertoire to produce antibodies of predetermined specificity. Nature, London 299:592–596
    [Google Scholar]
16. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
17. Müller H., Becht H. 1982; Biosynthesis of virus-specific proteins in cells infected with infectious bursal disease virus and their significance as structural elements for infectious virus and incomplete particles. Journal of Virology 44:384–392
    [Google Scholar]
18. Samson A. C. R., Willcocks M. M., Routledge E. G., Morgan L. A., Toms G. L. 1986; A neutralizing monoclonal antibody to respiratory syncytial virus which binds to both F₁ and F₂ components of the fusion protein. Journal of General Virology 67:1479–1483
    [Google Scholar]