Burroughs J N, Sangar D V, Clarke B E, Rowlands D J, Billiau A, Collen D
J Virol. 1984 Jun;50(3):878-83. doi: 10.1128/JVI.50.3.878-883.1984.
Translation of foot-and-mouth disease virus RNA in a rabbit reticulocyte lysate for short time intervals resulted in the production of the peptides P20a , P16, and P88 (Lab, Lb, and P1) (R. R. Rueckert , Recommendations of the 3rd European Study Group on Molecular Biology of Picornavirus, Urbino , Italy, 1983). If further translation was prevented, the structural protein precursor P88 was not cleaved, even after prolonged incubation. This result indicates that the mechanism of the cleavage between P20a -P16 and P88 and of that between P88 and P52 (P2) differs from the mechanism of the secondary cleavages which produce the structural proteins. Furthermore, treatment of foot-and-mouth disease virus-infected cells with the protease inhibitor D-valyl phenylalanyl lysyl chloromethyl ketone prevented the in vivo cleavage between P20a -P16 and P88 but had no effect on any of the other cleavage events. These results suggest that the cleavage of the foot-and-mouth disease virus polyprotein utilizes two different host proteases.
在兔网织红细胞裂解物中短时间间隔翻译口蹄疫病毒RNA可产生肽P20a、P16和P88（Lab、Lb和P1）（R.R.鲁克特，第三届欧洲小核糖核酸病毒分子生物学研究组建议，意大利乌尔比诺，1983年）。如果阻止进一步翻译，即使长时间孵育，结构蛋白前体P88也不会被切割。这一结果表明，P20a - P16与P88之间以及P88与P52（P2）之间的切割机制不同于产生结构蛋白的二级切割机制。此外，用蛋白酶抑制剂D-缬氨酰-苯丙氨酰-赖氨酰氯甲基酮处理口蹄疫病毒感染的细胞可阻止体内P20a - P16与P88之间的切割，但对任何其他切割事件均无影响。这些结果表明，口蹄疫病毒多聚蛋白的切割利用了两种不同的宿主蛋白酶。
