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口蹄疫病毒3C蛋白酶:抗病毒靶点的最新结构与功能见解

Foot-and-mouth disease virus 3C protease: recent structural and functional insights into an antiviral target.

作者信息

Curry Stephen, Roqué-Rosell Núria, Zunszain Patricia A, Leatherbarrow Robin J

机构信息

Biophysics Section, Division of Cell and Molecular Biology, Blackett Laboratory, Imperial College, Exhibition Road, London SW7 2AZ, UK.

出版信息

Int J Biochem Cell Biol. 2007;39(1):1-6. doi: 10.1016/j.biocel.2006.07.006. Epub 2006 Aug 14.

DOI:10.1016/j.biocel.2006.07.006
PMID:16979372
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7185863/
Abstract

The 3C protease from foot-and-mouth disease virus (FMDV 3C(pro)) is critical for viral pathogenesis, having vital roles in both the processing of the polyprotein precursor and RNA replication. Although recent structural and functional studies have revealed new insights into the mechanism and function of the enzyme, key questions remain that must be addressed before the potential of FMDV 3C(pro) as an antiviral drug target can be realised.

摘要

口蹄疫病毒的3C蛋白酶(FMDV 3C(pro))对病毒致病作用至关重要,在多聚蛋白前体加工和RNA复制过程中均发挥着关键作用。尽管最近的结构和功能研究揭示了该酶作用机制和功能的新见解,但在实现FMDV 3C(pro)作为抗病毒药物靶点的潜力之前,仍存在一些关键问题有待解决。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aaa6/7185863/c89ea5825f39/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aaa6/7185863/e775b5a10cc7/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aaa6/7185863/c89ea5825f39/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aaa6/7185863/e775b5a10cc7/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aaa6/7185863/c89ea5825f39/gr2.jpg

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本文引用的文献

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Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication.口蹄疫病毒3C蛋白的RNA结构和RNA结合活性在VPg尿苷酰化及病毒复制中的作用
J Virol. 2006 Oct;80(19):9865-75. doi: 10.1128/JVI.00561-06.
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X-ray crystallographic structure of the Norwalk virus protease at 1.5-A resolution.诺如病毒蛋白酶的X射线晶体结构,分辨率为1.5埃。
J Virol. 2006 May;80(10):5050-8. doi: 10.1128/JVI.80.10.5050-5058.2006.
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Dual modes of modification of hepatitis A virus 3C protease by a serine-derived beta-lactone: selective crystallization and formation of a functional catalytic triad in the active site.
口蹄疫病毒(FMDV)负调控 ZFP36 蛋白的表达,以减轻其抗病毒活性。
J Virol. 2024 Sep 17;98(9):e0111424. doi: 10.1128/jvi.01114-24. Epub 2024 Aug 28.
4
The antiviral response triggered by the cGAS/STING pathway is subverted by the foot-and-mouth disease virus proteases.cGAS/STING 通路触发的抗病毒反应被口蹄疫病毒蛋白酶颠覆。
Cell Mol Life Sci. 2024 Mar 20;81(1):148. doi: 10.1007/s00018-024-05190-7.
5
Structure-based virtual screening and molecular dynamics studies to explore potential natural inhibitors against 3C protease of foot-and-mouth disease virus.基于结构的虚拟筛选和分子动力学研究,以探索针对口蹄疫病毒3C蛋白酶的潜在天然抑制剂。
Front Vet Sci. 2024 Jan 17;10:1340126. doi: 10.3389/fvets.2023.1340126. eCollection 2023.
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丝氨酸衍生的β-内酰胺对甲型肝炎病毒3C蛋白酶的双重修饰模式:活性位点中选择性结晶及功能性催化三联体的形成
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Factors required for the Uridylylation of the foot-and-mouth disease virus 3B1, 3B2, and 3B3 peptides by the RNA-dependent RNA polymerase (3Dpol) in vitro.口蹄疫病毒3B1、3B2和3B3肽在体外被RNA依赖性RNA聚合酶(3Dpol)尿苷酸化所需的因素。
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Foot-and-mouth disease.口蹄疫
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