Stark R, Meyers G, Rümenapf T, Thiel H J
Federal Research Centre for Virus Diseases of Animals, Tübingen, Federal Republic of Germany.
J Virol. 1993 Dec;67(12):7088-95. doi: 10.1128/JVI.67.12.7088-7095.1993.
The polyprotein of classical swine fever virus starts with the nonstructural protein p23, which is followed by the nucleocapsid protein p14. Proteolytic cleavage between p23 and p14 was demonstrated in a cell-free transcription-translation system. Successive truncation of the cDNA used for the transcription indicated that the proteolytic activity responsible for the cleavage between p23 and p14 resides within p23. In order to determine the cleavage site between these two proteins, the respective genomic regions were expressed in two different expression systems. N-terminal sequencing of the resulting p14-related proteins revealed that cleavage occurs between Cys-168 and Ser-169. Comparison of the sequence around the cleavage site with sequences of other pestiviruses suggests a conserved processing site between similar proteins.
经典猪瘟病毒的多聚蛋白起始于非结构蛋白p23,随后是核衣壳蛋白p14。在无细胞转录-翻译系统中证实了p23和p14之间的蛋白水解切割。用于转录的cDNA的连续截短表明,负责p23和p14之间切割的蛋白水解活性存在于p23内。为了确定这两种蛋白之间的切割位点,在两种不同的表达系统中表达了各自的基因组区域。对所得p14相关蛋白的N端测序表明,切割发生在Cys-168和Ser-169之间。将切割位点周围的序列与其他瘟病毒的序列进行比较,提示相似蛋白之间存在保守的加工位点。