Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Patent
1996-04-12
1999-08-17
Fitzgerald, David L.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
424 854, 424 857, 530351, 536 2352, 4353201, C12N 1520, C07K 14555, A61K 3821
Patent
active
059392860
ABSTRACT:
The present invention describes hybrid interferon fusion polypeptides formed of a first segment that contains the N-terminal amino acid sequence of an interferon-tau polypeptide, and a second segment that contains the C-terminal amino acid sequence of a non-tau interferon type I polypeptide. The two segments are joined in the region of a mature interferon polypeptide between about residues 8 and 37. Also described are nucleic acid sequences encoding such interferon fusion polypeptides, expression vectors containing such sequences, and therapeutic applications of the interferon fusion polypeptides. The therapeutic applications include antiviral and anticellular proliferation applications. One advantage of the interferon fusion polypeptides of the present invention is that they do not have cytotoxic side-effects when used to treat cells.
REFERENCES:
patent: 4276282 (1981-06-01), Sugimoto et al.
patent: 4414150 (1983-11-01), Goeddel
patent: 4456748 (1984-06-01), Goeddel
patent: 4460574 (1984-07-01), Yabrov
patent: 4507281 (1985-03-01), Asculai et al.
patent: 4569908 (1986-02-01), Mark et al.
patent: 4636383 (1987-01-01), Nagabhushan et al.
patent: 4758428 (1988-07-01), Mark et al.
patent: 4846782 (1989-07-01), Bonnem
patent: 4874609 (1989-10-01), Rideout et al.
patent: 4892743 (1990-01-01), Leibowitz et al.
patent: 4897471 (1990-01-01), Stabinsky
patent: 4917887 (1990-04-01), Hauptman et al.
patent: 5019382 (1991-05-01), Cummins
patent: 5705363 (1998-01-01), Imakawa
patent: 5738845 (1998-04-01), Imakawa
Li, J., and Roberts, R.M., "Structure-Function Relationships in the Interferon-.tau. (IFN-.tau.): Changes in Receptor Binding and in Antiviral and Antiproliferative Activities Resulting from Site-Directed Mutagenesis Performed Near the Carboxyl Terminus," J. Biol. Chem. 269(40):24826-24833 (1994).
Soos, J.M., et al., "The IFN Pregnancy Recognition Hormone IFN-.tau. Blocks Both Development and Superantigen Reactivation of Experimental Allergic Encephalomyelitis Without Associated Toxicity," J. Immunol. 155:2747-2753 (1995).
Bazer, F.W., et al., "Role of Conceptus Secretory Products in Establishment of Pregnancy," J. Reprod. Fert. 76:841-850 (1986).
Bonnem, E.M., and Spiegel, R.J., "Interferon-.alpha.: Current Status and Future Promise," J. Biological Response Modifiers 3:580-598 (1984).
Godkin, et al., "Proteins Release by Cultured Day 15-16 Conceptuses Prolong Luteal Maintenance When Introduced into the Uterine Lumen of Cyclic Ewes," J. Reprod. Fertil. 71:57-64 (1984).
Imakawa, K., et al., "Interferon-Like Sequence of Ovine Trophoblast Protein Secreted by Embryonic Trophectoderm," Nature 330:377-379 (1987).
Jarpe, M.A., et al., "Predicted Structural Motif of IFN.tau.," Prot. Engin. 7(7):863-867 (1994).
Oldham, R.K., "Biologicals for Cancer Treatment: Interferons," Hosp. Pract. Dec. 15, pp. 71-86 (1985).
Ott, T.L., et al., "Cloning and Expression in Saccharomyces cerevisiae of a Synthetic Gene for the Type-I Trophoblast Interferon Ovine Trophoblast Protein-1: Purification and Antiviral Activity," J. Interferon Res. 11:357-364 (1991).
Pontzer, C.J., et al., "Antiviral Activity of the Pregnancy Recognition Hormone Ovine Trophoblast Protein-1," Biochem. Biophys. Res. Comm. 152:801-807 (1988).
Pontzer, C.J., et al., "Structure/Function Studies with Interferon Tau: Evidence for Multiple Active Sites," J. Interferon Res. 14:133-141 (1994).
Quesada, J.R., et al., "Alpha Interferon for Induction of Remission in Hairy-Cell Leukemia," N. Engl. J. Med. 310:15-18 (1984).
Salamonsen, L.A., et al., "Interferon-Alpha Mimics Effects of Ovine Trophoblast Protein 1 on Prostaglandin and Protein Secretion by Ovine Endometrial Cells In Vitro," J. Endocrin. 117:R1-R4 (1988).
Stewart, H.J., et al., "Interferon Sequence Homology and Receptor Binding Activity of Ovine Trophoblast Antileuteolytic Protein," J. Endicrinol. 115:R13-R15 (1987).
Subramaniam, P.S., et al., "Differential Recognition of the Type I Interferon Receptor by Interferons .tau. and .alpha. is Responsible for Their Disparate Cytotoxicities," Proc. Natl. Acad. Sci. USA 92:12270-12274 (1995).
Subramaniam, P.S., and Johnson, H.M., "Differential Recognition of the Type I Receptor by the Type I Interferons, IFN.tau. and IFN.alpha., is Responsible for Their Differential Cytotoxicities," FASEB J. 9(4):A1021 Abstract (1995).
White, et al., in Principles of Biochemistry, McGraw-Hill, New York, NY, 6th Edition, pp. 860-874 (1978).
Wilson, M.E., et al., "Proteins of Ovine Blastocyst Origin," Biol. Reproduct. 20(Sup 1):101A Abstract (1979).
Whaley, A.E., et al. (1994) J. Biol. Chem. 269: 10864-68.
Johnson Howard Marcellus
Pontzer Carol Hanlon
Subramaniam Prem Shankar
Dehlinger Peter J.
Fitzgerald David L.
Petithory Joanne R.
Sholtz Charles K.
University of Florida
LandOfFree
Hybrid interferon tau/alpha polypeptides, their recombinant prod does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Hybrid interferon tau/alpha polypeptides, their recombinant prod, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Hybrid interferon tau/alpha polypeptides, their recombinant prod will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-314363