Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Patent
1997-04-25
2000-07-04
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...
4352031, 435365, 4352523, 43525233, 43525411, 536 2352, 530351, 424 855, 4241981, 4241851, 424442, C12N 1523, C07K 1457, A61K 3821
Patent
active
060837241
DESCRIPTION:
BRIEF SUMMARY
The present invention relates generally to recombinant polypeptides having avian cytokine properties or avian cytokine-like properties and to genetic sequences encoding same. More particularly, the present invention is directed to recombinant avian Type II interferon polypeptides and specifically to avian interferon-.gamma. (IFN-.gamma.) and derivatives, homologues and analogues thereof and uses of same as an immune response modulator and as a growth enhancing agent.
Bibliographic details of the publications referred to in this specification by author are collected at the end of the description. Sequence Identity Numbers (SEQ ID NOs.) for the nucleotide and amino acid sequences referred to in the specification are defined following the bibliography.
Throughout this specification and the claims that follow, unless the context requires otherwise, the word "comprise", or variations such as "comprises" or "comprising" will be understood to imply the inclusion of a stated element or integer or group of elements or integers, but not the exclusion of any other element or integer or group of elements or integers.
The rapidly increasing sophistication of recombinant DNA technology is greatly facilitating research into the medical and veterinary fields. Cytokine research is of particular importance, especially as these molecules regulate the proliferation, differentiation and function of a great variety of cells, such as cells involved in mediating an immune response. Administration of recombinant cytokines or regulating cytokine function and/or synthesis is becoming, increasingly, the focus of medical research into the treatment of a range of disease conditions in humans and animals.
In mammals, interferons (IFN) represent a family of cytokines that share the capacity to inhibit viral replication and to exert effects on immune function. There are two distinct types of IFN. Type I IFN is produced by a variety of cell types in response to viral infection and includes IFN-.alpha. and -.beta.. Typically, IFN-.alpha. is produced by leukocytes such as monocytes and macrophages while fibroblasts and epithelial cells are the major source of IFN-.beta.. Type I IFNs share a high degree of amino acid homology, bind to the same cell surface receptor and there biological functions are resistant to heat and low pH treatment. (Weissmann and Weber, 1986)
In contrast, the production of Type II IFN-.gamma. in mammals is restricted to activated T cells and NK cells and is encoded by a gene that is unrelated to those which express IFN-.alpha. or IFN-.beta.. Features that distinguish IFN-.gamma. from -.alpha./.beta. include their binding to different cell surface receptors and that the former is exquisitely sensitive to heat and low pH treatment (Weissmann and Weber, 1986). Another distinction is the ability of IFN-.gamma., but not IFN-.alpha. or IFN-.beta., to stimulate macrophages to produce reactive nitrogen intermediates such as nitric oxide, nitrate and nitrite (Fast et al, 1993; Huang et al, 1993).
Chicken T cells produce IFN following stimulation with antigen or mitogen (Prowse and Pallister, 1989; Lowenthal et al, 1993; Pusztai et al, 1986; Weiler and von Bulow, 1987; Dijkmans et al, 1990) as measured by the ability to protect chick embryonic fibroblasts (CEF) from virus-mediated lysis. There has been controversy as to whether this IFN activity is the Type I or Type II equivalent of mammalian IFN (Lillehoj et al, 1992). In fact, the existence of IFN-.gamma. in avian species has been questioned (Dijkmans et al, 1990).
The gene for chicken Type I IFN (ChIFN-.alpha.) has recently been cloned (Sekellick et al, 1994) and when the protein was compared to mammalian IFNs it was shown to have 20-24% amino acid sequence identity to Type I IFNs, whereas it was unrelated to known mammalian IFN-.gamma. polypeptides. Furthermore, recombinant ChIFN-.alpha. was shown to have antiviral activity, but lacked macrophage activating function in that it was unable to induce nitrite secretion in monocytes (Schultz et al, 1995), consistent with the pro
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Schultz, et al., Eur. J. of Immunology, vol. 25, pp. 847-851 (1995) "Recombinant chicken interferon: a potent antiviral agent that lacks intrinsic macrophage activating factor activity".
Schultz, et al. Eur. J. of Biochemistry, vol. 229, pp. 73-76 (1995) "Recombinant chicken interferon from Escherichia coli and transfected COS cells is biologically active".
Weiler, H., et al. (1987) Avian Pathol. 16 : 439-52.
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Gray, et al., (1982) "Expression of human immune interferon cDNA in E. coli and monkey cells," Nature, 295:503-508.
Lillehoj, et al., (1993) "Avian Interleukin-2 and Interferon," Colloques De L'Inra (Avian Immunology In Progress), 62:105-111.
Lillehoj, et al., (1993) "Biochemical and functional characterizations of avian gamma-Interferon and Interleukin-2," Colloques De L'Inra (Avian Immunology In Progress), 62:131-136.
Lowenthal, et al., (1995) "Production of Interferon-gamma by chicken T cells," Journal of Interferon and Cytokine Research, 15:933-938.
Sekkellick, et al., (1994) "Chicken Interferon gene: Cloning, expression and analysis," Journal of Interferon Research, 14:71-79.
Weinig, et al, (1996) "Biological properties of recombinant chicken Interferon-gamma," European Journal of Immunology, 26:2440-2447.
Digby Matthew Robert
Lowenthal John William
O'Neil Terri Ellen
Rhodes Stephen
York Jennifer Joy
Commonwealth Scientific and Industrial Research Organization
Fitzgerald David L.
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