Meager A, Berg K
J Interferon Res. 1986 Dec;6(6):729-36. doi: 10.1089/jir.1986.6.729.
A murine monoclonal antibody, LO-22, with broad cross-reactivity to human interferon-alpha (HuIFN-alpha) subtypes and some animal IFN-alpha species was found to bind less efficiently to IFN-alpha A (IFN-alpha 2a). In contrast, LO-22 bound strongly to IFN-alpha 2 (IFN-alpha 2b) and IFN-alpha 2C (IFN-alpha 2c) which differ by one or two amino acids, respectively, from IFN-alpha A; the latter has lysine at position 23 whereas the other closely related IFNs have arginine. LO-22 also bound efficiently to IFN-alpha D which is only 83% related to IFN-alpha A, but which also has arginine at position 23. These results strongly suggest that LO-22 recognizes a conserved epitope among IFN-alpha 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.
发现一种对人α干扰素（HuIFN-α）亚型和一些动物α干扰素具有广泛交叉反应性的鼠单克隆抗体LO-22与IFN-α A（IFN-α 2a）的结合效率较低。相比之下，LO-22与IFN-α 2（IFN-α 2b）和IFN-α 2C（IFN-α 2c）强烈结合，它们与IFN-α A分别相差一个或两个氨基酸；后者在第23位有赖氨酸，而其他密切相关的干扰素在该位置有精氨酸。LO-22也能有效结合与IFN-α A仅有83%同源性但在第23位同样有精氨酸的IFN-α D。这些结果强烈表明，LO-22识别的是α干扰素亚型中一个保守的表位，其中第23位的精氨酸参与其中。还报告了第二种单克隆抗体MT4/E4的特异性，并将其与LO-22的特异性进行了比较。
