Herpes Simplex Virus Tegument ICP0 Is Capsid Associated, and Its E3 Ubiquitin Ligase Domain Is Important for Incorporation into Virions
Herpes Simplex Virus Tegument ICP0 Is Capsid Associated, and Its E3 Ubiquitin Ligase Domain Is Important for Incorporation into Virions
复制标题
DOI：
10.1128/jvi.02041-09
复制
发表时间：
2010-02-01
影响因子：
5.4
通讯作者：
Nicola, Anthony V.
中科院分区：
文献类型：
--
作者：
Delboy, Mark G.;Siekavizza-Robles, Carlos R.;Nicola, Anthony V.
单纯疱疹病毒(HSV)即刻早期(IE)蛋白ICP0是HSV感染的多功能调节因子。ICP0存在于被膜层中，但尚未得到很好的表征。野生型和ICP0缺失的病毒粒子的蛋白质组成相似，表明ICP0的缺失不会严重损害病毒粒子的组装。ICP0有一个具有E3泛素连接酶活性的环指结构域，这是IE功能所必需的。该结构域突变的病毒粒子包含的被膜ICP0水平大大降低，这表明该结构域影响ICP0的掺入。ICP0病毒粒子抵抗洗涤剂和盐的去除，并与衣壳有关，这是内被膜蛋白的共同特征。
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.