Donaghy G, Jupp R
Department of Biology, Roche Research Centre, Welwyn Garden City, Hertfordshire, United Kingdom.
J Virol. 1995 Feb;69(2):1265-70. doi: 10.1128/JVI.69.2.1265-1270.1995.
The BVRF2 gene of Epstein-Barr virus (EBV) shows homology to the UL26 and UL80 genes of herpes simplex virus type 1 (HSV-1) and cytomegalovirus (CMV), respectively. These genes are believed to provide a scaffold protein for the assembly of capsids leading to the formation of infectious viral particles. We have cloned the BVRF2 gene from the B95.8 strain of EBV and shown that the BVRF2 gene product is a polyprotein capable of autoproteolytic cleavage. Two Ala-Ser-containing recognition sequences were identified in the BVRF2 polyprotein at amino acid positions 568/569 and 570/571 where this cleavage was expected to occur. Here, we show that EBV proteinase is capable of cleaving at the first Ala-Ser bond but not the second. Comparison of the processing of the EBV and human CMV assembly domains in vitro by either EBV or human CMV proteinase revealed that, while both proteinases could cleave their native assembly domain, only EBV proteinase was able to cleave the assembly domain of the other virus.
爱泼斯坦-巴尔病毒(EBV)的BVRF2基因分别与单纯疱疹病毒1型(HSV-1)的UL26基因和巨细胞病毒(CMV)的UL80基因具有同源性。据信这些基因可为衣壳组装提供一种支架蛋白,从而导致感染性病毒颗粒的形成。我们从EBV的B95.8菌株中克隆了BVRF2基因,并表明BVRF2基因产物是一种能够进行自蛋白水解切割的多蛋白。在BVRF2多蛋白中,预期切割会发生的氨基酸位置568/569和570/571处鉴定出了两个含丙氨酸-丝氨酸的识别序列。在此,我们表明EBV蛋白酶能够在第一个丙氨酸-丝氨酸键处切割,但不能在第二个键处切割。通过EBV或人CMV蛋白酶对EBV和人CMV组装结构域在体外的加工过程进行比较,结果显示,虽然两种蛋白酶都能切割其天然组装结构域,但只有EBV蛋白酶能够切割另一种病毒的组装结构域。