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Bovine type I interferon receptor protein BoIFNAR‐1 has high‐affinity and broad specificity for human type I interferons
Author(s) -
Langer Jerome A,
Yang Jianliang,
Carmillo Paul,
Ling Leona E
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01550-0
Subject(s) - receptor , interferon , chemistry , type (biology) , biochemistry , biology , virology , ecology
The type I interferon receptor (IFNAR 1 ) is composed of two transmembrane polypeptides, IFNAR‐1 and IFNAR‐2. Human IFNAR‐1 has low intrinsic affinity for IFNs, but enhances the affinity for IFNs of the complex over that of HuIFNAR‐2 alone, and modulates the ligand specificity. Bovine cells respond to human alpha interferons. The bovine homologue of HuIFNAR‐1, BoIFNAR‐1, when expressed in heterologous cells, confers high‐affinity binding and broad specificity for human type I IFNs. A soluble fusion protein of the ectodomain of BoIFNAR‐1 and an immunoglobulin Fc domain was produced. In contrast to HuIFNAR‐1, this protein competes strongly with human cells for IFN binding, and directly binds a wide spectrum of human type I IFNs, including diverse IFN‐αs, IFN‐β and IFN‐ω, with moderate to high affinity. This accounts for much of the specificity for human IFNs possessed by bovine cells, with several exceptions. The BoIFNAR‐1 ectodomain, in contrast to HuIFNAR‐1, may be useful for studies of binary and ternary complexes with IFNs and IFNAR‐2, and for purification, assay and biological neutralization protocols.