A Bivalent Immunoadhesin of the Human Interferon-γ Receptor Is an Effective Inhibitor of IFN-γ Activity
| Autor: | Roland Hauff, Bodo Brocks, Klaus Pfizenmaier, Dieter Moosmayer, Elke Gerlach, Pascale De Becker |
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| Rok vydání: | 1995 |
| Předmět: |
Insecta
Recombinant Fusion Proteins Immunology Antibody Affinity Biology Protein Engineering Antiviral Agents Bivalent (genetics) Cell Line Interferon-gamma Species Specificity Antigens CD Virology Interferon-gamma receptor Extracellular Animals Humans Receptor Receptors Interferon Cell Biology Molecular biology Fusion protein Fragment crystallizable region In vitro Protein Structure Tertiary Solubility Biochemistry CD4 Immunoadhesins Alpha chain |
| Zdroj: | Journal of Interferon & Cytokine Research. 15:1111-1115 |
| ISSN: | 1557-7465 1079-9907 |
| DOI: | 10.1089/jir.1995.15.1111 |
| Popis: | We describe here the bioengineering of a bivalent IFN-gamma-RFc immunoadhesin consisting of the extracellular domain of the human IFN-gamma receptor alpha chain (IFN-gamma-R) fused to a human IgG1 Fc region (encoding hinge, CH2 and CH3 domain) that was efficiently expressed as a covalently linked homodimer in insect cells and purified in a one-step purification procedure. The IFN-gamma-RFc fusion protein exerted a 3-fold higher ligand binding affinity in binding competition studies in vitro compared with the monovalent extracellular IFN-gamma-R domain. In addition, the in vitro antagonistic activity of IFN-gamma-RFc, as determined by inhibition of IFN-gamma-induced virus protection and HLA-DR expression, was more than 30-fold higher in comparison with the monovalent soluble receptor. The described IFN-gamma-R immunoadhesin is a potential therapeutic reagent to interfere with the disease-promoting activities of IFN-gamma in several autoimmune diseases. |
| Databáze: | OpenAIRE |
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