Winkler M, Stamminger T
Institut für Klinische und Molekulare Virologie der Universität Erlangen-Nürnberg, Germany.
J Virol. 1996 Dec;70(12):8984-7. doi: 10.1128/JVI.70.12.8984-8987.1996.
The polypeptide encoded by the open reading frame UL69 of human cytomegalovirus (HCMV), which is homologous to the immediate-early regulator ICP27 of herpes simplex virus, has recently been identified as a transactivator protein that exerts a broad stimulatory effect on gene expression (M. Winkler, S. A. Rice, and T. Stamminger, J. Virol. 68:3943-3954, 1994). Here, we provide evidence that pUL69 is a phosphorylated tegument protein of HCMV. This finding could be demonstrated by Western blot (immunoblot) analyses with purified virions and a specific antiserum against pUL69. These experiments revealed that one phosphorylated subform of the three pUL69 polypeptides that are synthesized in infected fibroblast cells is contained within the HCMV virion. After the treatment of purified virions with detergents, pUL69 could not be detected within the membrane fraction, suggesting that it is either a capsid or a tegument protein. Its presence within dense bodies, however, shows that pUL69 is a constituent of the viral tegument.
人巨细胞病毒（HCMV）开放阅读框UL69编码的多肽与单纯疱疹病毒的立即早期调节因子ICP27同源，最近被鉴定为一种反式激活蛋白，对基因表达具有广泛的刺激作用（M. 温克勒、S. A. 赖斯和T. 施塔明格，《病毒学杂志》68:3943 - 3954，1994）。在此，我们提供证据表明pUL69是HCMV的一种磷酸化被膜蛋白。这一发现可通过用纯化病毒粒子和针对pUL69的特异性抗血清进行蛋白质印迹（免疫印迹）分析来证实。这些实验表明，在感染的成纤维细胞中合成的三种pUL69多肽中的一种磷酸化亚型存在于HCMV病毒粒子中。用去污剂处理纯化病毒粒子后，在膜组分中检测不到pUL69，这表明它要么是衣壳蛋白，要么是被膜蛋白。然而，它在致密体中的存在表明pUL69是病毒被膜的一个组成部分。
