Advertisement

Coronaviruses pp 351-363 | Cite as

Critical Epitopes in Transmissible Gastroenteritis Virus Neutralization

  • Luis Enjuanes
  • Isabel Correa
  • Gustavo Jiménez
  • Mercedes P. Melgosa
  • María J. Bullido
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 218)

Abstract

Transmissible gastroenteritis (TGE) virus induces neutralizing antibodies when virulent or attenuated (Bohl, 1981). In contrast, efective swine protection is only induced by virulent strains of the virus (Moxley and Olson, 1986), probably because these strains induce IgA or other serum factors that transfer protection to newborn littermates (Aynaud et al., 1986).

Keywords

Critical Epitope Antigenic Site Virus Neutralization African Swine Fever African Swine Fever Virus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. Aynaud, J.M., T.D. Nguyen, E. Bottreau, A. Brun, S. Bernard, and Ph. Vannier. 1986. Transmissible gastroenteritis: induction of a protective lactogenic immunity in the sow using the 188-SG strain of TGE virus (Nouzilly strain), p.189. C.Sánchez-Botija (ed.). Proceedings of the International Pig Veterinary Society 9th Congress. 9th IPVS Scientific Committee. Barcelona. Spain.Google Scholar
  2. Bohl, E.H. 1981. Transmissible gastroenteritis. p.168–208. In A.D. Leman, R.D. Glock, W.L. Mengeling, R.H.C. Penny, E. Scholl, B. Straw (ed.), Diseases of swine. Iowa State University Press. Ames.Google Scholar
  3. Chamberlain, J.P. 1979. Fluorographic detection of radioactivity in polyacrilamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98: 132–135.PubMedCrossRefGoogle Scholar
  4. Delmas, B., J. Gelfi, and H. Laude. 1986. Antigenic structure of transmissible gastroenteritis virus. II. Domains in the peplomer glycoprotein. J. gen. Virol. 67: 1405–1418.PubMedCrossRefGoogle Scholar
  5. Deschamps, J.R., J. E. K. Hildreth, D. Derp, and J.T. August. 1985. A high-perfomance liquid Chromatographic procedure for the purification of mouse monoclonal antibodies. Anal. Biochem. 147: 451–454.Google Scholar
  6. Geysen, H.M., S.J. Barteling, and R.H. Meloen. 1985. Small peptides induce antibodies with a sequence and structural requirements for binding antigen comparable to antibodies raised against the native protein. Proc. Natl. Acad. Sci. USA 82: 178–182.PubMedCrossRefGoogle Scholar
  7. Greenwod, F.C., W.M. Hunger, and J.W. Glover. 1963. The preparation of 131 I-labeled human growth hormone of high specific radioactivity. Biochem. J. 89: 114–123.Google Scholar
  8. Holland, J.J. 1984. Continuum of change in RNA virus genomes, p.137–143, in: “Concepts in viral pathogenesis”. Notkins, A.L., Oldstone, M.B.A., eds. Springer-Verlag, New York.CrossRefGoogle Scholar
  9. Hu, S., J. Bruszewski, T. Boone, and L. Souza. 1984. Cloning and expression of the surface glycoprotein gp 195 of porcine transmissible gastroenteritis virus, p. 219–223. In R.M. Chanock and R.A. Lerner (ed.), Modern approaches to vaccines. Cold Spring Harbor Laboratory. New York.Google Scholar
  10. Jiménez, G., I. Correa, M.P. Melgosa, M.J. Bullido, and L. Enjuanes. 1986. Critical epitopes in transmissible gastroenteritis virus neutralization. J. Virol. 60: 131–139PubMedGoogle Scholar
  11. Kearney, J.F., A. Radbruck, B. Liesegang, K. Rajewsky. 1979. A new mouse myeloma line which has lost immunoglobulin expression but permits the construction of antibody secreting hybrid cell lines. J. Immunol. 123: 1548–1550.PubMedGoogle Scholar
  12. Laude, H., J.M. Chapsal, and J. Gelfi, S. Labiau, and J. Grosclaude. 1986. Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins. J. Virol. 67: 119–130.CrossRefGoogle Scholar
  13. McClurkin, A.W., J.O. Norman. 1966. Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis. Can. J. Comp. Vet. Sci. 30: 190–198.Google Scholar
  14. Moxley, R.A., L.D. Olson. 1986. Comparison of TGE vaccines. p.191. In C. Sánchez-Botija (ed.), Proceedings of the International Pig Veterinary Society 9th Congress. 9th IPVS Congress Scientific Committee. Barcelona, Spain.Google Scholar
  15. Nowinski, R. C, M.E. Lostrom, M.R. Tarn., M.R. Stone, and W.N. Burnette. 1979. The isolation of hybrid cell line producing monoclonal antibodies against the p15(E) protein of murine leukemia viruses. Virology 93: 111–126.PubMedCrossRefGoogle Scholar
  16. Pierschbacher, M.D., and E. Ruoslahti. 1984. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309: 30–33.PubMedCrossRefGoogle Scholar
  17. Prabhakar, B.S., M.A. Menegus, and A.L. Notkins. 1985. Detection of conserved and nonconserved epitopes on Coxackievirus B4: frequency of antigenic change. Virology 146: 302–306.PubMedCrossRefGoogle Scholar
  18. Sanz, A., B. García-Barreno, M.L. Nogal, E. Viñuela, and L. Enjuanes. 1985. Monoclonal antibodies specific for African swine fever virus proteins. J. Virol. 54: 199–206.PubMedGoogle Scholar
  19. Sturman, L. S. 1981. The structure and behavior of coronavirus A59 glycoproteins. Adv. Exp. Med. Biol. 142: 1–17.PubMedGoogle Scholar
  20. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350–4354.PubMedCrossRefGoogle Scholar
  21. Wiktor, T.J., and H. Koprowski. 1980. Antigenic variants of rabies virus. J. Exp. Med. 152: 99–112.PubMedCrossRefGoogle Scholar
  22. Yewdell, J.W., A.J. Caton, and W. Gerhard. 1986. Selection of Influenza A virus adsorptive mutants by growth in the presence of a mixture of monoclonal antihemagglutinin antibodies. J. Virol. 57: 623–628.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Luis Enjuanes
    • 1
  • Isabel Correa
    • 1
  • Gustavo Jiménez
    • 1
  • Mercedes P. Melgosa
    • 1
  • María J. Bullido
    • 1
  1. 1.Centro de Biología MolecularC. S. I. C.-Universidad Autónoma, Canto BlancoMadridSpain

Personalised recommendations