Windisch J M, Schneider R, Stark R, Weiland E, Meyers G, Thiel H J
Institute of Biochemistry, University of Innsbruck, Austria.
J Virol. 1996 Jan;70(1):352-8. doi: 10.1128/JVI.70.1.352-358.1996.
The structural glycoprotein E0 of classical swine fever virus (CSFV) possesses an intrinsic RNase activity. Here we present the first comprehensive biochemical characterization of E0, using a recombinant glycoprotein expressed in insect cells. We were able to show that the presence of neither carbohydrate moieties nor disulfide bonds is a prerequisite for RNase activity. In addition, virus-neutralizing and nonneutralizing anti-E0 monoclonal antibodies were tested for their ability to influence RNase activity. In these experiments, the antibodies which effectively blocked the infection of STE cells also exerted a high degree of E0 RNase inhibition. This correlation suggests that the RNase activity of CSFV E0 plays a role in the viral life cycle.
经典猪瘟病毒(CSFV)的结构糖蛋白E0具有内在的核糖核酸酶活性。在此,我们利用在昆虫细胞中表达的重组糖蛋白,首次对E0进行了全面的生化特性分析。我们能够证明,碳水化合物部分和二硫键的存在都不是核糖核酸酶活性的先决条件。此外,还测试了病毒中和及非中和抗E0单克隆抗体影响核糖核酸酶活性的能力。在这些实验中,有效阻断STE细胞感染的抗体也对E0核糖核酸酶有高度抑制作用。这种相关性表明,CSFV E0的核糖核酸酶活性在病毒生命周期中发挥作用。