人疱疹病毒6型蛋白酶的克隆、表达及特性分析
Cloning, expression and characterization of the proteinase from human herpesvirus 6.
作者信息
Tigue N J, Matharu P J, Roberts N A, Mills J S, Kay J, Jupp R
机构信息
Department of Molecular and Medical Biosciences, University of Wales College of Cardiff, United Kingdom.
出版信息
J Virol. 1996 Jun;70(6):4136-41. doi: 10.1128/JVI.70.6.4136-4141.1996.
Abstract
After the U53 gene encoding the proteinase from human herpesvirus 6 (HHV-6) was sequenced, it was expressed in Escherichia coli, and the activity of the purified, recombinant HHV-6 proteinase was characterized quantitatively by using synthetic peptide substrates mimicking the release and maturation cleavage sites in the polyprotein precursors of HHV-6, human cytomegalovirus (CMV), murine CMV, and Epstein-Barr virus. Despite sharing 40% identity with other betaherpesvirus proteinases such as human CMV proteinase, the one-chain HHV-6 enzyme was distinguished from these two-chain proteinases by the absence of an internal autocatalytic cleavage site.
摘要
对编码人疱疹病毒6型（HHV-6）蛋白酶的U53基因进行测序后，将其在大肠杆菌中表达，并通过使用模拟HHV-6、人巨细胞病毒（CMV）、鼠巨细胞病毒和爱泼斯坦-巴尔病毒多蛋白前体中释放和成熟切割位点的合成肽底物，对纯化的重组HHV-6蛋白酶的活性进行了定量表征。尽管与其他β疱疹病毒蛋白酶如人CMV蛋白酶有40%的同源性，但单链HHV-6酶与这些双链蛋白酶的区别在于没有内部自催化切割位点。
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