C-terminally truncated interferon

Details C-terminally truncated interferon C-terminally truncated interferon

2011-03-29

2011-03-29

Worley, Cathy Kingdon (Department: 1638)

Multicellular living organisms and unmodified parts thereof and

Method of introducing a polynucleotide molecule into or...

Nonplant protein is expressed from the polynucleotide

C800S278000, C800S280000, C800S294000, C800S295000, C800S298000, C536S023520, C435S419000, C435S320100

Reexamination Certificate

active

07915483

ABSTRACT:
The invention described herein provides a C-terminally truncated interferon having a deletion of 7, 8, or 9 amino acids and having enhanced biological activity, and the polynucleotides encoding such an interferon. Also provided are methods for producing and using such truncated interferon. In some embodiments, the truncated interferon is produced in a plant.

REFERENCES:
patent: 4956282 (1990-09-01), Goodman et al.
patent: 5550038 (1996-08-01), Goodman et al.
patent: 5629175 (1997-05-01), Goodman et al.
patent: 6040498 (2000-03-01), Stomp et al.
patent: 6096547 (2000-08-01), Goodman et al.
patent: 6610830 (2003-08-01), Goeddel et al.
patent: 6774283 (2004-08-01), Goodman et al.
patent: 6815184 (2004-11-01), Stomp et al.
patent: 7161064 (2007-01-01), Stomp et al.
patent: 2002/0088027 (2002-07-01), Stomp et al.
patent: 2003/0115640 (2003-06-01), Stomp et al.
patent: 2003/0135887 (2003-07-01), Brandle et al.
patent: 2003/0167531 (2003-09-01), Russell et al.
patent: 2004/0073968 (2004-04-01), Stomp et al.
patent: 2004/0219131 (2004-11-01), Patten et al.
patent: 2005/0060776 (2005-03-01), Stomp et al.
patent: 2005/0221344 (2005-10-01), Welcher et al.
patent: 2006/0195946 (2006-08-01), Dickey et al.
patent: 2007/0044177 (2007-02-01), Stomp et al.
patent: 2007/0128162 (2007-06-01), Dickey et al.
patent: 2009/0282584 (2009-11-01), Stomp et al.
patent: 393690 (1991-11-01), None
patent: 0032134 (1981-07-01), None
patent: 0141484 (1985-05-01), None
patent: 0 194 006 (1986-09-01), None
patent: 0 256 424 (1988-02-01), None
patent: WO 01/36001 (2001-05-01), None
patent: WO 02 10414 (2002-02-01), None
patent: WO 02 43650 (2002-06-01), None
patent: WO 03/002152 (2003-01-01), None
patent: WO 2004/046365 (2004-06-01), None
patent: WO 2005/035767 (2005-04-01), None
Sugyiama et al. Expression of human interferon-a2 in Sf9 cells.(1993) Eur. J. Biochem; vol. 217; pp. 921-927.
Zhu et al. Expression of human a-interferon cDNA in transgenic rice plants. (1994) Plant Cell, Tissue and Organ Culture; vol. 36; pp. 197-204.
Schillberg et al. Review—Molecular farming of recombinant antibodies in plants. (2003) CMLA, Cell. Mol. Life Sci.; vol. 60; pp. 433-445.
Ahn et al. A novel extensin gene encoding a hydroxyproline-rich glycoprotein requires sucrose for its wound-inducible expression in transgenic plants. (1996) The Plant Cell; vol. 8; pp. 1477-1490.
Ackerman, S.K., et al., Biologic Activity in a Fragment of Recombinant Human Interferon α,Proc. Natl. Acad. Sci., USA, 1984, pp. 1045-1047, vol. 81.
Chang, N. T., et al., “Synthesis of a Human Leukocyte Interferon with a Modified Carboxy Terminus inEscherichia coli,” Archives of Biochemistry and Biophysics, 1983, pp. 585.
Chang, et al., “Evolution of a cytokine using DNA family shuffling”,Nature Biotech. (1999) 17:793-797.
Cheetham, B.F., et al., “Structure-Function Studies of Human Interferons-α: Enhanced Activity on Human and Murine Cells,”Antiviral Research, 1991, pp. 27-40, vol. 15.
Cohen, “The manipulation of genes”,Scientific American(1975) pp. 25-33.
Franke, A.E., et al., “Carboxyterminal Region of Hybrid Leukocyte Interferons Affects Antiviral Specificity,” DNA, 1982, vol. 1(3).
Gasdaska, J.R., et al., Advantages of Therapeutic Protein Production in the Aquatic PlantLemna, www.bioprocessingjournal.com, Mar./Apr. 2003.
Green, et al., “Isolation and cell-free translation of immunoglobulin messenger RNA”,Arch. of Biochem. and Biophy. (1976) 172:74-89.
Guarente, et al., “Improved methods for maximizing expression of a cloned gene: a bacterium that synthesizes rabbit beta-globin”,Cell(1980) 20:543-553.
Guarente, et al., “A technique for expressing eukaryotic genes in bacteria”,Science(1980) 209(4463):1428-1430.
Houghton, “Human interferon gene sequences”,Nature(1980) 285(5766):536.
Itakura, et al., “Expression inE. coliof a chemically synthesized gene for the hormone somatostatin”,Science(1977) 198(4321):1056-1063.
Levy, et al., “Amino acid sequence of a human leukocyte interferon”,Proc. Natl. Acad. Sci. USA(1981) 78(10):6186-6190.
Mantei, et al., “The nucleotide sequence of a cloned human leukocyte interferon cDNA”,Gene(1980) 10:1-10.
Mantei, et al., “The nucleotide sequence of a cloned human leukocyte interferon cDNA”,Chemical Abstracts(1980) 93:489, Abstract No. 130319s.
Miller, “Use of recombinant DNA technology for the production of polypeptides”,Adv. Exp. Med. Biol. (1979) 118:153-174.
Nagata, et al., “The structure of one of the eight or more distinct chromosomal genes for human intereferon-alpha”,Nature(1980) 287(5781):401-408.
Nagata, et al., “Synthesis inE. coliof a polypeptide with human leukocyte interferon activity”,Chemical Abstracts(1980) 93:479, Abstract No. 41286m.
Nagata, et al., “Synthesis inE. coliof a polypeptide with human leukocyte interferon activity”,Nature(1980) 284:316-320.
Ozes, et al., “A comparison of Interferon-Con1 with natural recombinant interferons-alpha: antiviral, antiproliferative, and natural killer-inducing activities”,J. Interferon Res. (1992) 12:55-59.
Pestka and Langer, “Interferons and their actions”,Ann. Rev. Biochem. (1987) 56:727-77.
Platis and Foster, “High yield expression, refolding, and characterization of recombinant interferon α2/α8 hybrids inEscherichia coli”, Protein Expression and Purfication(2003) 31:222-230.
Prouty, et al., “Degradation of abnormal proteins inEscherichia coli”, J. Bio. Chem. (1975) 250(3):1112-1122.
Roberts, et al., “Synthesis of Simian Virus 40 t Antigen inEscherichia coli”, Proc. Natl. Acad. Sci. USA(1979) 76(11):5596-5600.
Roberts, et al., “A General Method for Maximizing the Expression of a Cloned Gene”,Proc. Natl. Acad. Sci. USA(1979) 76(2):760-764.
Rubinstein, et al., “Human leukocyte interferon: isolation and characterization of several molecular forms”,Arch. of Biochem. and Biophysics(1981) 210:307-318.
Rubinstein, et al., “Human leukocyte interferon purified to homogeneity”,Science(1978) 202(4374):1289-1290.
Rubinstein, et al., “Human leukocyte interferon: production, purification to homogeneity, and initial characterization”,Proc. Natl. Acad. Sci. USA(1979) 76(2):640-644.
Schouten, et al., “Improving scFv antibody expression levels in the plant cytosol”,FEBS Letters(1997) 415:235-241.
Staehelin, et al., “Production of Hybridomas Secreting Monoclonal Antibodies to the Human Leukocyte Interferons”,Proc. Natl. Acad. Sci. USA(1981) 78(3):1848-1852.
Stebbing, et al., “Biological comparison of natural and recombinant DNA-derived polypeptides”,State of the Art: Insulin and Growth Hormone(1980) pp. 12-21.
Streuli, et al., “At least three human type alpha interferons: structure of alpha 2”,Science(1980) 209(4463):1343-1347.
Taniguchi, et al., “Expression of the Human Fibroblast Interferon Gene inEscherichia coli”, Proc. Natl. Acad. Sci. USA(1980) 77(9):5230-5233.
Taniguchi, et al., “Human leukocyte and fibroblast interferons are structurally related”,Nature(1980) 285:547-549.
Torma and Paucker, “Purification and characterization of human leukocyte interferon components”,J. Biol. Chem. (1976) 251(16):4810-4816.
Weissmann, “The cloning of interferon and other mistakes”,Interferon(1981) 3:101-134.
Zoon, et al., “Amino terminal sequence of the major component of human lymphoblastoid interferon”,Science(1980) 207(4430):527-528.
Zoon, et al., “Purification and partial characterization of human lymphoblastoid interferon”,Proc. Natl. Acad. Sci. USA(1979) 76(11):5601-5605.
Zoon, et al., “Human lymphoblastoid interferon: purification, amino acid composition, and amino-terminal sequence”,Ann. NY Acad. Sci. (1980) 350:390-398.
Arnheiter, H., et al.,

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