Antibodies against IFN γ-Binding Proteins Recognize a Member of IFN α R Complex

• Published in: Biochemical and biophysical research communications Vol. 280; no. 4; pp. 1197 - 1202
• Main Authors: Bello, Iraldo, Rodes, Lorenzo, Saura, Pedro Lopez
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 02.02.2001
• Subjects: Antibodies, Monoclonal - metabolism; Blotting, Western; Cell Membrane - chemistry; Cell Membrane - metabolism; conformational epitopes; Electrophoresis, Polyacrylamide Gel; Epitopes; Humans; IFN binding; IFN α; IFN-γR1; IFNAR2; Interferon-gamma - immunology; Membrane Proteins; Placenta - metabolism; Protein Binding; Protein Conformation; Receptor, Interferon alpha-beta; Receptors, Interferon - chemistry; Receptors, Interferon - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; shared structures; Silicon Dioxide - chemistry; IFNAR2; IFN-γR1; conformational epitopes; IFN binding; IFN α; shared structures
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.2000.4198

Recombinant human IFN α 2b coupled to a silica support was used for the purification of the IFN α-binding proteins from placental cell membrane extracts. The 100-kDa (p100) and 64-kDa (p64) proteins, which bind preferentially to an IFN α 2b-silica matrix, were identified. Using a monoclonal antibody (A6) against IFN-γR1, it was able to isolate p100 and p70, but only if IFN α 2b was present during chromatography. Similar interactions were observed using polyclonal antibody anti-IFN γ binding proteins, as assayed in Western blot. These interactions were identified as conformation dependent. We speculate that IFN α 2b receptor complex shares an IFN γ receptor complex epitope.