Buchholz C J, Gerlier D, Hu A, Cathomen T, Liszewski M K, Atkinson J P, Cattaneo R
Institut fur Molekularbiologie, Abteilung I, Hönggerberg, Universität, Zürich, Switzerland.
Virology. 1996 Mar 1;217(1):349-55. doi: 10.1006/viro.1996.0122.
The human cell surface protein CD46 is the main measles virus (MV) receptor. We analyzed the CD46 isoforms expressed in the brain of three patients who died with persistent MV infections and in an unaffected brain. Complete CD46 cDNAs were produced and found to code exclusively for CD46 isoforms with cytoplasmic tail 2. Selective expression of tail 2 isoforms was shown in a second control brain by Western blots with antibodies specific for each of the cytoplasmic tails. Binding of purified MV particles and virus-dependent cell fusion were tested after transient expression of brain-derived CD46 proteins in mouse cells. All the brain-derived proteins mediated MV binding and virus-dependent fusion. Isoforms containing both serine/threonine/proline (STP)-rich domains were more active in virus binding, whereas isoforms with only one STP domain were more efficient in mediating fusion.
人类细胞表面蛋白CD46是主要的麻疹病毒(MV)受体。我们分析了三名死于持续性MV感染患者的大脑以及一个未受感染大脑中表达的CD46亚型。制备了完整的CD46 cDNA,发现其仅编码具有细胞质尾2的CD46亚型。通过使用针对每个细胞质尾的特异性抗体进行蛋白质印迹,在第二个对照大脑中显示了尾2亚型的选择性表达。在小鼠细胞中瞬时表达脑源性CD46蛋白后,测试了纯化的MV颗粒的结合以及病毒依赖性细胞融合。所有脑源性蛋白均介导MV结合和病毒依赖性融合。含有富含丝氨酸/苏氨酸/脯氨酸(STP)结构域的亚型在病毒结合方面更具活性,而仅具有一个STP结构域的亚型在介导融合方面更有效。