单纯疱疹病毒外壳 ICP0 与衣壳相关，其 E3 泛素连接酶结构域对于病毒粒子的组装很重要。
Herpes simplex virus tegument ICP0 is capsid associated, and its E3 ubiquitin ligase domain is important for incorporation into virions.
机构信息
Department of Microbiology and Immunology, School of Medicine, Virginia Commonwealth University, Richmond, Virginia 23298-0678, USA.
出版信息
J Virol. 2010 Feb;84(3):1637-40. doi: 10.1128/JVI.02041-09. Epub 2009 Nov 11.
Abstract
Herpes simplex virus (HSV) immediate-early (IE) protein ICP0 is a multifunctional regulator of HSV infection. ICP0 that is present in the tegument layer has not been well characterized. Protein compositions of wild-type and ICP0 null virions were similar, suggesting that the absence of ICP0 does not grossly impair virion assembly. ICP0 has a RING finger domain with E3 ubiquitin ligase activity that is necessary for IE functions. Virions with mutations in this domain contained greatly reduced levels of tegument ICP0, suggesting that the domain influences the incorporation of ICP0. Virion ICP0 was resistant to removal by detergent and salt and was associated with capsids, features common to inner tegument proteins.
摘要
单纯疱疹病毒 (HSV) 早期即刻 (IE) 蛋白 ICP0 是 HSV 感染的多功能调节剂。位于衣壳层的 ICP0 尚未得到很好的表征。野生型和 ICP0 缺失病毒粒子的蛋白组成相似，表明 ICP0 的缺失不会严重损害病毒粒子的组装。ICP0 具有 RING 指结构域和 E3 泛素连接酶活性，这对于 IE 功能是必需的。该结构域发生突变的病毒粒子中，衣壳层 ICP0 的含量大大降低，这表明该结构域影响 ICP0 的掺入。病毒粒子 ICP0 能抵抗去污剂和盐的去除，并与衣壳相关联，这是内部衣壳蛋白的共同特征。
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