Anti-Idiotypes and Lymphokine Receptors: Interferon as a Model

  • Phyllis L. Osheroff

Abstract

Anti-idiotypic antibodies have been used as cell surface receptor probes in a number of systems (for a review, see Ref. 1). However, there have been relatively few reports which describe monoclonal anti-idiotypic antibodies that not only recognize the receptors specific for a protein or polypeptide but also trigger the known biological activity of that protein or polypeptide. The biological and potential clinical significance of various lymphokines and the generally low level of expression of cellular receptors for these biologically active proteins make the study of anti-idiotypes as probes for these lymphokine receptors especially interesting and important. The successful cloning of various human interferon cDNAs and their expression in bacteria (for a review, see Ref. 2), coupled with recent reports showing direct analysis of interferon binding to specific cellular receptors (for a review, see Ref. 3), enabled us to use the recombinant human leukocyte A interferon (rIFN-aA) as a model system to study the anti-idiotypes as interferon receptor probes. This model system can be applied to studies of receptors for other lymphokines or biologically active proteins.

Keywords

Antiviral Activity Receptor Binding Site Human Interferon MDBK Cell Normal Mouse Serum 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Strosberg, A.D., J.G. Guillet, S. Chamat, and J. Hoebeke. 1985. Recognition of physiological receptors by anti-idiotypic antibodies: molecular mimicry of the ligand or cross-reactivity ? Curr. Top. Microbiol. Immunol. 119: 91.Google Scholar
  2. 2.
    Pestka, S. 1983. The human interferons—from protein purification and sequence to cloning and expression in bacteria: before, between, and beyond. Arch. Biochem. Biophys. 221: 1.Google Scholar
  3. 3.
    Aguet, M. and K.E. Mogensen. 1983. Interferon receptors, pp. 1-22. In I. Gresser (ed.), Interferon 1983, Vol. 5. Academic Press, New York.Google Scholar
  4. 4.
    Friedman, R.M. 1981. Interferons: a primer. Academic Press, New York.Google Scholar
  5. 5.
    Stewart, W.E., II. 1979. The interferon system. Springer-Verlag, New York.Google Scholar
  6. 6.
    Taniguchi, T., N. Mantei, M. Schwarzstein, S. Nagata, M. Muramatsu, and C. Weissmann. 1980. Human leukocyte and fibroblast interferons are structurally related. Nature 285: 547.PubMedCrossRefGoogle Scholar
  7. 7.
    Goeddel, D.V., D.W. Leung, T.J. Dull, M. Gross, R.M. Lawn, R. McCandliss, P.H. Seeburg, A. Ullrich, E. Yelverton, and P. Gray. 1981. The structure of eight distinct cloned human leukocyte interferon cDNAs. Nature 294: 768.CrossRefGoogle Scholar
  8. 8.
    Branca, A.A., and C. Baglioni. 1981. Evidence that type I and II interferons have different receptors. Nature (London) 294: 768.CrossRefGoogle Scholar
  9. 9.
    Anderson, P., Y.K. Yip, and J. Vilcek. 1982. Specific binding of l2T-human interferon-7 to high affinity receptors on human fibroblasts. J. Biol. Chem. 259: 11301.Google Scholar
  10. 10.
    Rehberg, E., B. Kelder, E. Hoal, and S. Pestka. 1982. Specific molecular activities of recombinant and hybrid leukocyte interferons. J. Biol. Chem. 257: 11497.PubMedGoogle Scholar
  11. 11.
    Aguet, M., M. Grobke, and P. Dreiding. 1984. Various human interferon a subclasses cross-react with common receptors: their binding affinities correlate with their specific biological activities. Virology 132: 211.PubMedCrossRefGoogle Scholar
  12. 12.
    Uze, G., K.E. Mogensen, and M. Aguet. 1985. Receptor dynamics of closely related ligands: “fast” and “slow” interferons. EMBO J. 4: 65.PubMedGoogle Scholar
  13. 13.
    Staehelin, T., B. Durrer, J. Schmidt, B. Takacs, J. Stocker, V. Miggiano, C. Stahli, M. Rubinstein, W.P. Levy, R. Hershberg, and S. Pestka. 1981. Pro¬duction of hybridomas secreting monoclonal antibodies to the human leukocyte interferons. Proc. Natl. Acad. Sci. USA 78: 1848.PubMedCrossRefGoogle Scholar
  14. 14.
    Staehelin, T., D.S. Hobbs, H.-F. Kung, C.-Y. Lai, and S. Pestka. 1981. Purification and characterization of recombinant human leukocyte interferon (IFLrA) with monoclonal antibodies. J. Biol. Chem. 256: 9750.PubMedGoogle Scholar
  15. 15.
    Rubinstein, S., P.C. Familletti, and S. Pestka. 1981. Convenient assay for interferons. J. Virol. 37: 755.PubMedGoogle Scholar
  16. 16.
    Takemori, T., H. Tesch, M. Reth, and K. Rajewsky. 1982. The immune response against anti-idiotope antibodies. I. Induction of idiotope-bearing antibodies and analysis of the idiotope repertoire. Eur. J. Immunol. 12: 1040.Google Scholar
  17. 17.
    Stocker, J.W., H.K. Forster, V. Miggiano, C. Stahli, G. Staiger, B. Takacs, and T. Staehelin. 1982. Generation of 2 new mouse myeloma cell lines “PAI” and “PAI-O” for hybridoma production. Research Disclosure 1982: 155.Google Scholar
  18. 18.
    Zola, H., and D. Brooks. 1982. Techniques for the production and characterization of monoclonal hybridoma antibodies, pp. 1-57. In J.G. Hurrell (ed.), Monoclonal hybridoma antibodies: techniques and applications. CRC Press, Boca Raton, Florida.Google Scholar
  19. 19.
    Osheroff, P.L., T.-R. Chiang and D. Manousos. 1985. Interferon-like activity in an antfcinterferon anti-idiotypic hybridoma antibody. J. Immunol. 135: 306.PubMedGoogle Scholar
  20. 20.
    Zoon, K., D.Z. Nedden, and H. Arnheiter. 1982. Specific binding of human a interferon to a high affinity cell surface binding site on bovine kidney cells. J. Biol. Chem. 257: 4695.PubMedGoogle Scholar
  21. 21.
    Gibson, A.L., J.N. Herron, D.W. Ballard, E.W. Voss, Jr., X.M. He, V.A. Patrick, and A.B. Edmundson. 1985. Crystallographic characterization of the Fab fragment of a monoclonal anti-ss-DNA antibody. Mol. Immunol. 22: 499.Google Scholar
  22. 22.
    Edmundson, A.B., and K.R. Ely. 1985. Binding of AMormylated chemotactic peptides in crystals of the Meg light chain dimer: similarities with neutrophil receptors. Mol. Immunol. 22: 463.Google Scholar

Copyright information

© Springer-Verlag New York Inc. 1988

Authors and Affiliations

  • Phyllis L. Osheroff

There are no affiliations available

Personalised recommendations