The Role of Three Domains in the Biological Activity of Human Interferon-α

Journal of Interferon Research

Volumn 9, Issue 1, 1989, Pages 97-114

  Fish, E N ^a   Banerjee, K ^a   Stebbing, N ^b  

^a UNIVERSITY OF TORONTO   (Canada)

^b AKZO NOBEL CENTRAL RESEARCH   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

2',5' OLIGOADENYLATE SYNTHETASE; ALPHA INTERFERON DERIVATIVE; BETA INTERFERON; MONOCLONAL ANTIBODY;

ANIMAL CELL; CELL CULTURE; DRUG RECEPTOR BINDING; HAMSTER; HUMAN; HUMAN CELL; MONKEY; MOUSE; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

2',5'-OLIGOADENYLATE SYNTHETASE; AMINO ACID SEQUENCE; CELLS, CULTURED; ENZYME INDUCTION; GROWTH INHIBITORS; HUMAN; INTERFERON TYPE I; PREDICTIVE VALUE OF TESTS; PROTEIN CONFORMATION; RECEPTORS, IMMUNOLOGIC; RECEPTORS, INTERFERON; SUPPORT, NON-U.S. GOV'T; TUMOR CELLS, CULTURED;

EID: 0024502589     PISSN: 01978357     EISSN: 15577465     Source Type: Journal    
DOI: 10.1089/jir.1989.9.97     Document Type: Article

References (42)

1. STEWART II, W.E. (1981). In: The Interferon System, 2nd ed. New York: Springer-Verlag.
2. Wetzel, R., Levine, H.L., Estell, D.A., Shire, S., FINER-Moore, J., Stroud, R.M., and Bewley, T.A. (1982). Structure-function studies on human alpha interferon. UCLA Symp. Mol. Cell. Biol. XXV, 365–376, Academic Press.
3. Morehead, H., Johnston, P.D., and Wetzel, R. (1984). Roles of the 19–138 disulfide bond of subtype A of human α interferon in its antiviral activity and conformational stability. Biochemistry 23, 2500–2507.
4. Smith, M.E., Komoriya, A., and Anfinsen, C.B. (1981). Target cell specificity of two species of human interferon-α produced in Escherichia coli and of hybrid molecules derived from them, in: The Biology of the Interferon System. E. De Maeyer, G. Galasso, and H. Schellekens (eds.). Amsterdam: Elsevier/North-Holland Biomedical Press, pp. 39–42.
5. Arnheiter, H., Thomas, R.M., Leist, T., Fountoulakis, M., and Gutte, B. (1981). Physicochemical and antigenic properties of synthetic fragments of human leukocyte interferon. Nature 294, 278–280.
6. Zoon, K., ZUR Nedden, D., and Arnheiter, H. (1982). Specific binding of human α interferon to a high affinity cell surface binding site on bovine kidney cells. J. Biol. Chem. 257, 4695–4697.
7. Ackerman, S.K., ZUR Nedden, D., Heintzelman, M., Hunkapiller, M., and Zoon, K. (1984). Biologic activity in a fragment of recombinant human interferon α. Proc. Natl. Acad. Sci. USA 81, 1045–1047.
8. Arnheiter, H., Ohno, M., Smith, M., Gutte, B., and Zoon, K.C. (1983). Orientation of human leukocyte interferon molecule on its cell surface receptor: Carboxyl terminus remains accessible to monoclonal antibody made against a synthetic interferon fragment. Proc. Natl. Acad. Sci. USA 80, 2539–2543.
9. Adolf, G.R. (1987). Antigenic structure of human interferon ω1 (interferon α11): Comparison with other human interferons. J. Gen. Virol. 68, 1669–1676.
10. Weck, P.K., Stebbing, N., Gray, P.W., Leung, D., Shepard, H.M., and Goeddel, D.V. (1981). Antiviral activities of hybrids of two major leukocyte interferons. Nucleic Acids Res. 9, 6153–6156.
11. Streuli, M., Hall, A., Boll, W., STEWART II, W.E., Nagata, S., and Weissman, C. (1981). Target cell specificity of two species of human interferon-α produced in Escherichia coli and of hybrid molecules derived from them. Proc. Natl. Acad. Sci. USA 78, 2848–2852.
12. Rehberg, E., Kelder, B., Hoal, G., and Pestka, S. (1982). Specific molecular activities of recombinant and hybrid leukocyte interferons. J. Biol. Chem. 257, 11497–11502.
13. Franke, A.E., Shepard, H.M., Houck, C.M., Leung, D.W., Goeddel, D.V., and Lawn, R.M. (1982). Carboxyterminal region of hybrid leukocyte interferons affects antiviral specificity. DNA 1, 223–230.
14. Chang, N.T., Kung, H.-F., and PESTKA. S. (1983). Synthesis of a human leukocyte interferon with a modified carboxy terminus in Escherichia coli. Arch. Biochem. Biophys. 221, 585–589.
15. Meister, A., Uze, G., Mogensen, K.E., Gresser, I., Tovey, M.G., Grutter, M.U., and Meyer, F. (1986). Biologic activities and receptor binding of two human recombinant interferons and their hybrids. J. Gen. Virol. 67, 1633–1643.
16. Weber, H., Valenzuela, D., Lujber, G., and Weissman, C. (1987). Single amino acid changes that render human IFN-α2 biologically active on mouse cells. EMBO J. 6, 591–598.
17. Shafferman, A., Velan, B., Cohen, S., Leitner, M., and Grosfeld, H. (1987). Specific residues within an amino-terminal domain of 35 residues of interferon α are responsible for recognition of the human interferon α cell receptor and for triggering biological effects. J. Biol. Chem. 262, 6227–6237.
18. Alton, K., Stabinsky, Y., Richards, R., Ferguson, B., Goldstein, L., Altrock, B., Miller, L., and Stebbing, N. (1983). Production, characterization and biological effects of recombinant DNA derived human IFN-α and IFN-γ analogs, in: The Biology of the Interferon System 1983. E. De Maeyer and H. Schellekens (eds.). Amsterdam: Elsevier. pp. 119–128.
19. Edge, M.D., Camble, R., Moore, V.E., Hockney, R.C., Carr, F.J., and Fitton, J.E. (1986). In: Interferon 7, I. Gresser (ed.). Academic Press, pp. 1–46.
20. Valenzuela, D., Weber, H., and Weissman, C. (1985). Is sequence conservation in interferons due to selection for functional proteins? Nature 313, 698–700.
21. Nisbet, I.T., Beilharz, M.W., Hertzog, P.J., Tymms, M.J., and Linnane, A.W. (1985). Single amino acid substitutions at conserved residues of human interferon-α can affect antiviral specific activity. Biochem. Int. 11, 301–309.
22. Camble, R., Petter, N.N., Trueman, P., Newton, C.R., Carr, F.J., Hockney, R.C., Moore, V.E., Greene, A.R., Holland, D., and Edge, M. (1986). Functionally important conserved amino-acids in interferon-α2 identified with analogues produced from synthetic genes. Biochem. Biophys. Res. Commun. 134, 1404–1411.
23. Marcucci, F., and DE Maeyer, E. (1986). An interferon analogue IAla30,32,33I HuIFN-α2, acting as a HuIFN-α2 antagonist on bovine cells. Biochem. Biophys. Res. Commun. 134, 1413–1418.
24. Fish, E.N., Banerjee, K., and Stebbing, N. (1983). Human leukocyte interferon subtypes have different antiproliferative and antiviral activities on human cells. Biochem. Biophys. Res. Commun. 112, 537–546.
25. Altrock, B.W., Chang, D., Fish, E.N., Hockman, H.R., and Duker, K. (1986). Antibody defined active regions of human interferons, in: UCLA Symposium on Immune Regulation by Characterized Polypeptides, vol. 41. G. Goldstein, J.F. Bach, and H. Wigzell (eds.). New York: Alan R. Liss.
26. Goeddel, D.V., Leung, D.W., Dull, T.J., Gross, M., Lawn, R.M., Mccandliss, R., Seeburg, P.H., Ullrich, A., Yelverton, E., and Gray, P.W. (1981). The structure of eight distinct cloned human leukocyte interferon cDNAs. Nature 290, 20–26.
27. Weck, P.K., Apperson, S., May, L., and Stebbing, N. (1981). Comparison of the antiviral activities of various cloned human interferon-alpha subtypes in mammalian cell cultures. J. Gen. Virol. 57, 233–237.
28. Penn, L.J.Z., and Williams, B.R.G. (1984). Interferon-induced 2–5A synthetase activity in human peripheral blood mononuclear cells after immunization with influenza virus and rubella virus vaccines. J. Virol. 49, 748–753.
29. Hannigan, G.E., Gewert, D.R., Rish, E.N., Read, S.E., and Williams, B.R.G. (1983). Differential binding of human interferon-α subtypes to receptors on lymphoblastoid cells. Biochem. Biophys. Res. Comun. 110, 537–544.
30. Hannigan, G.E., Fish, E.N., and Williams, B.R.G. (1984). Modulation of human interferon-α receptor expression by human interferon-γ. J. Biol. Chem. 259, 8084–8086.
31. Wolf, H., Modrow, S., Motz, M., Jameson, B., Hermann, G., and Fortsch, B. (1988). The antigenic index: A novel algorithm for predicting antigenic determinants. CABIOS 4, 181–186.
32. Wolf, H., Modrow, S., Motz, M., Jameson, B., Hermann, G., and Fortsch, B. (1988). An integrated family of amino acid sequence analysis programmes. CABIOS 4, 187–191.
33. Chou, P.Y., and Fasman, G.D. (1974). Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins., Biochemistry 13, 211–222.
34. Garnier, J., Osguthorpe, D.J., and Robson, B. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97–120.
35. Engelman, D.M., Steitz, T.A., and Goldman, A. (1986). Identifying non-polar transbilayer helices in amino acid sequences of membrane proteins. Ann. Rev. Biophys. Chem. 15, 321–353.
36. Eisenberg, D., Sweet, R.M., and Terwilleger, T.C. (1984). The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. USA 81, 140–144.
37. Kyte, J., and Doolittle, R.F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105–132.
38. Emini, E.A., Hughes, J.V., Perlow, D.S., and Boger, J. (1985). Induction of hepatitis A virus neutralizing antibody by virus-specific synthetic peptide. J. Virol. 55, 836–839.
39. Karplus, P.A., and Shulz, G.E. (1985). Prediction of chain flexibility in proteins. Naturwissenschaften 72, 212–213.
40. Dreiding, P., Staeheli, P., and Haller, O. (1983). Interferon-induced protein Mx accumulates in nuclei of mouse cells expressing resistance to influenza viruses. Virology 140, 192–196.
41. Horovitz, O., Rubinstein, M., and Revel, M. (1985). Two regions of the human IFN-αC molecule involved in binding to the human cell receptor, in: The Biology of the Interferon System, E. De Maeyer and H. Schellekens (eds.). Amsterdam: Elsevier. pp. 157–162.
42. Fish, E.N., Banerjee, K., Arakawa, T., and Stebbing, N. (1988). Structure/function studies on recombinant human gamma interferon. Drug Design Deliv. 2, 191–206.