一种在即刻早期2蛋白中具有磷酸化位点突变的人巨细胞病毒的特性分析。
Characterization of a human cytomegalovirus with phosphorylation site mutations in the immediate-early 2 protein.
作者信息
Heider Julie A, Yu Yongjun, Shenk Thomas, Alwine James C
机构信息
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014, USA.
出版信息
J Virol. 2002 Jan;76(2):928-32. doi: 10.1128/jvi.76.2.928-932.2002.
Abstract
A human cytomegalovirus mutant (TNsubIE2P) was constructed with alanine substitutions of four residues (T27, S144, T233, and S234) previously shown to be phosphorylated in the immediate-early 2 (IE2) protein. This mutant grew as well as the wild type at both low and high multiplicities of infection. The mutant activated the major immediate-early, UL4, and UL44 promoters to similar levels, and with similar kinetics, as wild-type virus. However, the TNsubIE2P mutant virus transactivated an endogenous simian virus 40 early promoter 4 h earlier and to higher levels than the wild-type virus in infected human fibroblasts. The modification of the IE2 protein by SUMO-1 (i.e., its sumoylated state) was also examined.
摘要
构建了一种人巨细胞病毒突变体（TNsubIE2P），其对先前显示在即刻早期2（IE2）蛋白中发生磷酸化的四个残基（T27、S144、T233和S234）进行了丙氨酸替换。该突变体在低感染复数和高感染复数下的生长情况与野生型相同。该突变体激活主要即刻早期、UL4和UL44启动子的水平和动力学与野生型病毒相似。然而，在感染的人成纤维细胞中，TNsubIE2P突变体病毒比野生型病毒提前4小时反式激活内源性猿猴病毒40早期启动子，且激活水平更高。还检测了IE2蛋白被SUMO-1修饰的情况（即其SUMO化状态）。
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