Abstract
A murine monoclonal antibody, LO-22, with broad cross-reactivity to human interferon-α (HuIFN-α) subtypes and some animal IFN-α species was found to bind less efficiently to IFN-αA (IFN-α2a*). In contrast, LO-22 bound strongly to IFN-α2 (IFN-α2b*) and IFN-α2C (IFN-α2c*) which differ by one or two amino acids, respectively, from IFN-α; the latter has lysine at position 23 whereas the other closely related IFNs have arginine. LO-22 also bound efficiently to IFN-αD which is only 83% related to IFN-αA, but which also has arginine at position 23. These results strongly suggest that LO-22 recognizes a conserved epitope among IFN-α subtypes in which arginine at position 23 is involved. The specificity of a second monoclonal antibody, MT4/E4, is also reported and compared to that of LO-22.
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