Carter M J
Department of Virology, University of Newcastle-upon-Tyne, New Medical School, U.K.
Arch Virol. 1989;108(1-2):69-79. doi: 10.1007/BF01313744.
We have used Western blotting to examine the accumulation of feline calicivirus proteins within the infected cell. Experiments using elevated growth temperature to block post-translational cleavage have demonstrated two additional high molecular weight protein bands 125 kd and 123 kd respectively which may be precursor polyproteins. Inhibition of proteolytic processing with p-fluorophenylalanine led to the accumulation of several additional protein species which may represent intermediates in the protein processing pathway. None of these proteins were related to the 62 kd major capsid protein (cP62) of the virus as judged by reaction with monoclonal antibodies. The production of a 76 kd capsid precursor protein (cpP 76) was demonstrated for the first time in FCV-infected cells. The pathway by which calicivirus polypeptides are made thus appears highly complex and may involve temporal regulation of protein synthesis as well as protein processing. Tentative identification of primary, intermediate and mature forms of virus proteins is discussed.
我们已使用蛋白质印迹法来检测猫杯状病毒蛋白在受感染细胞内的积累情况。利用升高生长温度来阻断翻译后切割的实验表明，分别出现了两条额外的高分子量蛋白条带，分子量分别为125kd和123kd，它们可能是前体多聚蛋白。用对氟苯丙氨酸抑制蛋白水解加工导致了几种额外蛋白质种类的积累，这些蛋白质可能代表蛋白质加工途径中的中间体。通过与单克隆抗体反应判断，这些蛋白质均与该病毒的62kd主要衣壳蛋白（cP62）无关。首次在感染猫杯状病毒的细胞中证实了76kd衣壳前体蛋白（cpP 76）的产生。因此，杯状病毒多肽的产生途径似乎高度复杂，可能涉及蛋白质合成的时间调控以及蛋白质加工。文中还讨论了病毒蛋白初级、中间和成熟形式的初步鉴定。
