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本文引用的文献

1
Ribonuclease multiplicity, diversity, and complexity.核糖核酸酶的多样性、差异性和复杂性。
J Biol Chem. 1993 Jun 25;268(18):13011-4.
2
Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects.核糖核酸酶III对噬菌体T7加工信号的切割。二价阳离子特异性及特定阴离子效应。
Nucleic Acids Res. 1993 Apr 25;21(8):1919-25. doi: 10.1093/nar/21.8.1919.
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Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model for the reaction intermediate.
Eur J Biochem. 1993 Aug 15;216(1):301-5. doi: 10.1111/j.1432-1033.1993.tb18145.x.
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Processing of the envelope glycoproteins of pestiviruses.瘟病毒包膜糖蛋白的加工过程。
J Virol. 1993 Jun;67(6):3288-94. doi: 10.1128/JVI.67.6.3288-3294.1993.
5
Identification of a structural glycoprotein of an RNA virus as a ribonuclease.鉴定一种RNA病毒的结构糖蛋白为核糖核酸酶。
Science. 1993 Aug 27;261(5125):1169-71. doi: 10.1126/science.8356450.
6
Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera.在昆虫细胞中表达的猪霍乱病毒糖蛋白E1可保护猪免受猪霍乱的侵害。
J Virol. 1993 Sep;67(9):5435-42. doi: 10.1128/JVI.67.9.5435-5442.1993.
7
Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus.瘟病毒多聚蛋白的加工：经典猪瘟病毒自身蛋白酶与核衣壳蛋白之间的切割位点
J Virol. 1993 Dec;67(12):7088-95. doi: 10.1128/JVI.67.12.7088-7095.1993.
8
Glycoprotein E2 of classical swine fever virus: expression in insect cells and identification as a ribonuclease.经典猪瘟病毒糖蛋白E2：在昆虫细胞中的表达及作为核糖核酸酶的鉴定
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Loss of a histidine residue at the active site of S-locus ribonuclease is associated with self-compatibility in Lycopersicon peruvianum.番茄中S-位点核糖核酸酶活性位点处组氨酸残基的缺失与自交亲和性相关。
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猪瘟病毒的核糖核酸酶：生化特性及病毒中和单克隆抗体对其的抑制作用

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

作者信息

Windisch J M, Schneider R, Stark R, Weiland E, Meyers G, Thiel H J

机构信息

Institute of Biochemistry, University of Innsbruck, Austria.

出版信息

J Virol. 1996 Jan;70(1):352-8. doi: 10.1128/JVI.70.1.352-358.1996.

DOI:10.1128/JVI.70.1.352-358.1996
PMID:8523547
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC189824/
Abstract

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.

摘要

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。