Wolf D G, Honigman A, Lazarovits J, Tavor E, Panet A
Department of Clinical Microbiology and Infectious Diseases, Hadassah University Hospital Jerusalem, Israel.
Arch Virol. 1998;143(6):1223-32. doi: 10.1007/s007050050370.
The cellular localization and virion association of the human cytomegalovirus (HCMV) UL97 protein were studied. UL97 protein demonstrated early nuclear localization followed by late perinuclear accumulation. It was found to be a structural virion constituent detected in all three enveloped forms of extracellular viral particles and shown to be phosphorylated by the virion-associated protein kinase. UL97 protein immunoprecipitated from virions and from infected cells demonstrated protein kinase activity manifested by autophosphorylation. This activity was reduced in the presence of a ganciclovir-resistance mutation at residue 460, implicated in nucleotide binding. A mutant virus, from which the proposed UL97 kinase catalytic domain had been deleted, could not be propagated in the absence of a helper wild-type virus. The characterization of UL97 protein as a virion-associated protein kinase which appears essential for viral replication, provides further insight into HCMV replication and could identify a potential novel target for antiviral therapy.
对人巨细胞病毒（HCMV）UL97蛋白的细胞定位和病毒体关联进行了研究。UL97蛋白表现出早期核定位，随后在核周晚期积累。发现它是在细胞外病毒颗粒的所有三种包膜形式中检测到的一种结构病毒体成分，并显示被病毒体相关蛋白激酶磷酸化。从病毒体和感染细胞中免疫沉淀的UL97蛋白表现出通过自身磷酸化体现的蛋白激酶活性。在第460位残基存在与核苷酸结合有关的更昔洛韦抗性突变的情况下，这种活性降低。一种缺失了提议的UL97激酶催化结构域的突变病毒，在没有辅助野生型病毒的情况下无法增殖。将UL97蛋白鉴定为一种对病毒复制似乎至关重要的病毒体相关蛋白激酶，为深入了解HCMV复制提供了进一步的线索，并可能确定一个潜在的抗病毒治疗新靶点。
