Everett R, Orr A, Elliott M
MRC Virology Unit, Institute of Virology, Glasgow, UK.
J Gen Virol. 1995 Sep;76 ( Pt 9):2369-74. doi: 10.1099/0022-1317-76-9-2369.
All alpha herpesviruses of known DNA sequence have been found to encode a protein with similarities to immediate early protein Vmw110 (ICP0) of herpes simplex virus type 1 (HSV-1). The conserved portion of this family of proteins is a characteristic zinc binding module, known as a RING finger or C3HC4 domain. Examples of RING finger domains occur in many other proteins of diverse evolutionary origin and function. Recently, the solution structure of the equine herpesvirus 1 (EHV-1) RING finger protein, encoded by gene 63, has been solved. To investigate whether this structure could be considered to be a paradigm of herpesvirus RING domains, we have constructed a recombinant HSV-1 which expresses the EHV-1 gene 63 protein (EHVg63) in place of Vmw110. Comparison of the growth properties of the recombinant with those of wild-type and Vmw110-defective viruses indicates that EHVg63 is able to fulfil partially, but not completely, the roles of Vmw110 during virus growth in tissue culture.
所有已知DNA序列的甲型疱疹病毒都被发现编码一种与1型单纯疱疹病毒（HSV-1）的立即早期蛋白Vmw110（ICP0）相似的蛋白质。该蛋白家族的保守部分是一个特征性的锌结合模块，称为环指或C3HC4结构域。环指结构域存在于许多其他具有不同进化起源和功能的蛋白质中。最近，由基因63编码的马疱疹病毒1型（EHV-1）环指蛋白的溶液结构已被解析。为了研究这种结构是否可被视为疱疹病毒环结构域的范例，我们构建了一种重组HSV-1，它表达EHV-1基因63蛋白（EHVg63）来替代Vmw110。将重组病毒与野生型病毒和Vmw110缺陷型病毒的生长特性进行比较，结果表明EHVg63在组织培养中的病毒生长过程中能够部分但不能完全发挥Vmw110的作用。
