Jalanko A
FEBS Lett. 1985 Jul 1;186(1):59-64. doi: 10.1016/0014-5793(85)81339-9.
Here, the proteolytic processing of the Semliki Forest virus (SFV) capsid protein was studied in the absence of other viral functions. Two different fragments of the SFV messenger cDNA, coding for capsid protein and 174 and 38 extra amino acids from the envelope proteins, respectively, were cloned in the late region of the SV40 viral DNA. Cells infected with the SV40 recombinant virus stocks were analyzed for the production of SFV capsid mRNA and polypeptide. Immunofluorescence staining of the infected cells indicated that the produced SFV capsid protein accumulated mainly in the nucleus. Polyacrylamide gel electrophoresis of the immunoprecipitated SFV capsid proteins showed that both recombinants yielded a labelled band equivalent in size to the SFV capsid protein. Thus the proteolytic processing takes place even under conditions where the capsid protein is the only virus-specified protein synthesized.
在此,在不存在其他病毒功能的情况下研究了塞姆利基森林病毒(SFV)衣壳蛋白的蛋白水解加工过程。分别编码衣壳蛋白以及来自包膜蛋白的174个和38个额外氨基酸的两个不同的SFV信使cDNA片段被克隆到SV40病毒DNA的晚期区域。对感染了SV40重组病毒株的细胞进行分析,以检测SFV衣壳mRNA和多肽的产生。对感染细胞的免疫荧光染色表明,所产生的SFV衣壳蛋白主要积聚在细胞核中。对免疫沉淀的SFV衣壳蛋白进行聚丙烯酰胺凝胶电泳显示,两种重组体均产生了一条大小与SFV衣壳蛋白相当的标记条带。因此,即使在衣壳蛋白是唯一合成的病毒特异性蛋白的条件下,蛋白水解加工过程也会发生。