Banham A H, Smith G L
Sir William Dunn School of Pathology, University of Oxford, United Kingdom.
Virology. 1992 Dec;191(2):803-12. doi: 10.1016/0042-6822(92)90256-o.
Vaccinia virus open reading frame B1R was expressed in E. coli and shown to encode a serine/threonine protein kinase which phosphorylated casein and calf thymus histones in vitro. A polyclonal rabbit antiserum was raised against a TrpE-B1R bacterial fusion protein and used to characterize the B1R gene product. Immunoprecipitation and immunoblotting analyses detected a 34-kDa polypeptide that was synthesized early during vaccinia virus infection and which was apparently stable since it was easily detectable 18 hr postinfection. Immunofluorescence demonstrated that this protein localizes in cytoplasmic virus factories, the sites of virus DNA replication. Immunoblotting of vaccinia virions showed that the enzyme is packaged into virus particles.
痘苗病毒开放阅读框B1R在大肠杆菌中表达,并显示其编码一种丝氨酸/苏氨酸蛋白激酶,该激酶在体外可使酪蛋白和小牛胸腺组蛋白磷酸化。针对TrpE - B1R细菌融合蛋白制备了兔多克隆抗血清,并用于鉴定B1R基因产物。免疫沉淀和免疫印迹分析检测到一种34 kDa的多肽,它在痘苗病毒感染早期合成,并且显然是稳定的,因为在感染后18小时很容易检测到。免疫荧光显示该蛋白定位于细胞质病毒工厂,即病毒DNA复制的位点。痘苗病毒粒子的免疫印迹表明该酶被包装到病毒颗粒中。