A monoclonal antibody to recombinant human IFN-alpha receptor inhibits biologic activity of several species of human IFN-alpha, IFN-beta, and IFN-omega. Detection of heterogeneity of the cellular type I IFN receptor.

摘要: A cDNA encoding a 63-kDa human IFN-alpha R (hIFN-alpha R) has recently been cloned. Mouse cells transfected with this failed to show any signal transmission for IFN-beta, suggesting the involvement of additional chains in receptor complex. We have expressed Escherichia coli and COS 7 soluble recombinant protein (sIFN-alpha comprising extracellular domain hIFN-alpha fused at carboxyl terminus sequence five histidine residues. The sIFN-alpha was affinity purified used generate mAb. One mAb, 64G12, which recognized cellular as well proteins found neutralize biologic activity IFN-alpha, -beta, -omega natural type I IFN, but not IFN-gamma. To our knowledge, is first report neutralizing mAb against R. Interestingly, we that antibody depended on cell line used. These results provide strong evidence cloned chain required binding all subspecies IFN suggest structural heterogeneity surface.