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Intrinsic ligand binding properties of the human and bovine alpha-interferon receptors
1Department of Molecular Genetics & Microbiology, UDMNJ-Robert Wood Johnson Medical School, Piscataway 08854.
The Type I interferon receptor (IFN-alpha R) interacts with all IFN-alpha s, IFN-beta and IFN-omega, and seems to be a multisubunit receptor. To investigate the role of a cloned receptor subunit (IFN-alpha R1), we have examined the intrinsic ligand binding properties of the bovine and human IFN-alpha R1 polypeptides expressed in Xenopus laevis oocytes. Albeit with different efficiencies, Xenopus oocytes expressing either the human or bovine IFN-alpha R1 polypeptide exhibit significant binding and formation of crosslinked complexes with human IFN-alpha A and IFN-alpha B. Thus, the IFN-alpha R1 polypeptide most likely plays a direct role in ligand binding.
The Type I interferon receptor (IFN-alpha R) interacts with all IFN-alpha s, IFN-beta and IFN-omega, and seems to be a multisubunit receptor. To investigate the role of a cloned receptor subunit (IFN-alpha R1), we have examined the intrinsic ligand binding properties of the bovine and human IFN-alpha R1 polypeptides expressed in Xenopus laevis oocytes. Albeit with different efficiencies, Xenopus oocytes expressing either the human or bovine IFN-alpha R1 polypeptide exhibit significant binding and formation of crosslinked complexes with human IFN-alpha A and IFN-alpha B. Thus, the IFN-alpha R1 polypeptide most likely plays a direct role in ligand binding.