Ono N, Tatsuo H, Tanaka K, Minagawa H, Yanagi Y
Department of Virology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan.
J Virol. 2001 Feb;75(4):1594-600. doi: 10.1128/JVI.75.4.1594-1600.2001.
Human signaling lymphocytic activation molecule (SLAM; also known as CDw150) has been shown to be a cellular receptor for measles virus (MV). Chinese hamster ovary cells transfected with a mouse SLAM cDNA were not susceptible to MV and the vesicular stomatitis virus pseudotype bearing MV envelope proteins alone, indicating that mouse SLAM cannot act as an MV receptor. To determine the functional domain of the receptor, we tested the abilities of several chimeric SLAM proteins to function as MV receptors. The ectodomain of SLAM comprises the two immunoglobulin superfamily domains (V and C2). Various chimeric transmembrane proteins possessing the V domain of human SLAM were able to act as MV receptors, whereas a chimera consisting of human SLAM containing the mouse V domain instead of the human V domain no longer acted as a receptor. To examine the interaction between SLAM and MV envelope proteins, recombinant soluble forms of SLAM were produced. The soluble molecules possessing the V domain of human SLAM were shown to bind to cells expressing the MV hemagglutinin (H) protein but not to cells expressing the MV fusion protein or irrelevant envelope proteins. These results indicate that the V domain of human SLAM is necessary and sufficient to interact with the MV H protein and allow MV entry.
人类信号淋巴细胞激活分子（SLAM；也称为CDw150）已被证明是麻疹病毒（MV）的细胞受体。用小鼠SLAM cDNA转染的中国仓鼠卵巢细胞对MV以及仅携带MV包膜蛋白的水泡性口炎病毒假型不敏感，这表明小鼠SLAM不能作为MV受体。为了确定受体的功能结构域，我们测试了几种嵌合SLAM蛋白作为MV受体的功能。SLAM的胞外结构域由两个免疫球蛋白超家族结构域（V和C2）组成。具有人SLAM的V结构域的各种嵌合跨膜蛋白能够作为MV受体，而由包含小鼠V结构域而非人V结构域的人SLAM组成的嵌合体不再作为受体起作用。为了研究SLAM与MV包膜蛋白之间的相互作用，制备了重组可溶性形式的SLAM。具有人SLAM的V结构域的可溶性分子被证明能与表达MV血凝素（H）蛋白的细胞结合，但不能与表达MV融合蛋白或无关包膜蛋白的细胞结合。这些结果表明，人SLAM的V结构域对于与MV H蛋白相互作用并允许MV进入是必要且充分的。
