Abstract
Interferons (IFNs) are a class of proteins, secreted by animal cells in response to various inducers1, which confer resistance to viral infections and are designated according to their cellular origin or to the inducing agent. Viruses induce type I Interferon, subdivided into α-interferon, produced by leukocytes (Le) or lymphoblastoid (Ly) cells, and β-interferon, produced by fibroblasts1. Mitogens and antigenic stimuli induce in lymphocytes type II immune IFN-γ. Interferons seem to bind to specific receptors2 to elicit a variety of cellular responses3; several early studies provided indirect evidence for such binding4–6. Direct evidence for specific interferon receptors was presented by Aguet7, who showed that biologically active 125I-labelled mouse (Mu)IFN binds to sensitive L1210-S cells, but not to interferon-resistant L1210-R cells8. The main obstacle in carrying out such studies is the availability of pure interferon. Recently, Maeda et al.9 constructed plasmids containing human interferon sequences. The plasmid p104 was used as a probe to isolate the coding region of a human interferon (IFLrA), which was expressed in Escherichia coli10 and purified with monoclonal antibodies11. This interferon, designated HuIFN-αA, was labelled with 125I for binding assays on human cells. We have determined the specificity of different HuIFNs for the cellular sites which bind HuIFN-αA and show here that HuIFN-γ does not compete for binding, whereas all type I HuIFNs do.
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Branca, A., Baglioni, C. Evidence that types I and II interferons have different receptors. Nature 294, 768–770 (1981). https://doi.org/10.1038/294768a0
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DOI: https://doi.org/10.1038/294768a0
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