Monoclonal antibodies to the human interferon-γ receptor: blocking of the biological activities of interferon-γ and purification of the receptor

D Novick, DG FISCHER, ZVI REITER… - Journal of interferon …, 1989 - liebertpub.com
D Novick, DG FISCHER, ZVI REITER, Z Eshhar, M Rubinstein
Journal of interferon research, 1989liebertpub.com
Monoclonal antibodies against the human interferon-γ (IFN-γ) receptor were developed by
injecting mice with a preparation of receptor that was purified from solubilized placental
membranes by ligand affinity chromatography. Three antibodies were identified by their
ability to block the binding of 125I-labeled IFN-γ to its receptor on HeLa cells at 4° C. One of
these antibodies blocked several biological activities of IFN-γ, including its antiviral activity,
its ability to induce HLA-DR surface antigens, and its ability to protect cells from NK cell …
Abstract
Monoclonal antibodies against the human interferon-γ (IFN-γ) receptor were developed by injecting mice with a preparation of receptor that was purified from solubilized placental membranes by ligand affinity chromatography. Three antibodies were identified by their ability to block the binding of 125I-labeled IFN-γ to its receptor on HeLa cells at 4°C. One of these antibodies blocked several biological activities of IFN-γ, including its antiviral activity, its ability to induce HLA-DR surface antigens, and its ability to protect cells from NK cell-mediated cytotoxicity. This antibody exhibited higher binding capacity to cells at 37°C and was significantly less displaceable by an excess of IFN-γ as compared with the other two antibodies. Immunoaffinity chromatography of solubilized crude placental membrane preparation yielded a purified receptor that exhibited a molecular weight of 88,000. The purified receptor retained its ability to bind 125I-labeled IFN-γ in solution.
Mary Ann Liebert