RNase of classical swine fever virus: Biochemical characterization and inhibition by virus-neutralizing monoclonal antibodies

被引:72
|
作者
Windisch, JM
Schneider, R
Stark, R
Weiland, E
Meyers, G
Thiel, HJ
机构
[1] UNIV GIESSEN, INST VIROL, D-35392 GIESSEN, GERMANY
[2] UNIV INNSBRUCK, INST BIOCHEM, A-6020 INNSBRUCK, AUSTRIA
[3] FED RES CTR VIRUS DIS ANIM, D-72076 TUBINGEN, GERMANY
关键词
D O I
10.1128/JVI.70.1.352-358.1996
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 mono clonal 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.
引用
收藏
页码:352 / 358
页数:7
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