Purves F C, Longnecker R M, Leader D P, Roizman B
J Virol. 1987 Sep;61(9):2896-901. doi: 10.1128/JVI.61.9.2896-2901.1987.
Earlier reports have described a novel protein kinase in cells infected with herpes simplex or pseudorabies viruses. These novel enzymes were characterized by their acceptance of protamine as a substrate and by their differential chromatographic behavior in anion-exchange chromatography. We report that this activity was not present in extracts of uninfected cells or of cells infected with a mutant constructed so as to contain a deletion in the US3 open reading frame mapping in the small component of herpes simplex virus 1 DNA. The activity was present in extracts of cells infected with wild-type virus and with a recombinant in which the US3 open reading frame had been rescued. Our results are consistent with the observation reported earlier that the coding sequences predict an amino acid motif common to protein kinases and lead to the conclusion that the US3 open reading frame encodes a virus-specific protein kinase that is not required for virus growth in cells in culture.
早期报告描述了在感染单纯疱疹病毒或伪狂犬病病毒的细胞中存在一种新型蛋白激酶。这些新型酶的特点是能将鱼精蛋白作为底物，并且在阴离子交换色谱中具有不同的色谱行为。我们报告称，这种活性在未感染细胞的提取物中不存在，在感染了构建的突变体的细胞提取物中也不存在，该突变体在单纯疱疹病毒1型DNA小成分中的US3开放阅读框中存在缺失。这种活性存在于感染野生型病毒的细胞提取物以及US3开放阅读框已被挽救的重组体感染的细胞提取物中。我们的结果与早期报道的观察结果一致，即编码序列预测出蛋白激酶共有的氨基酸基序，并得出结论：US3开放阅读框编码一种病毒特异性蛋白激酶，而在培养细胞中病毒生长不需要该激酶。
