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将水疱性口炎病毒核糖核蛋白显微注射到动物细胞中可产生有感染性的病毒。

Microinjection of vesicular stomatitis virus ribonucleoprotein into animal cells yields infectious virus.

作者信息

Thornton G B, Kopchick J J, Stacey D W, Banerjee A K

出版信息

Biochem Biophys Res Commun. 1983 Nov 15;116(3):1160-7. doi: 10.1016/s0006-291x(83)80264-2.

DOI:10.1016/s0006-291x(83)80264-2
PMID:6316970
Abstract

Microinjection of purified transcriptionally active ribonucleoprotein (RNP) complex of vesicular stomatitis virus in vero cells resulted in the production and release of virus. Compared to the release of virus by cells treated with RNP in the presence of DEAE-dextran, the microinjection technique was highly efficient. Microinjection in Xenopus oocytes also resulted in initiation of infection as shown by the synthesis of virus-specific proteins in the cell cytoplasm. It was further observed that RNP stripped of L protein but containing residual NS protein was capable of initiating virus production or protein synthesis when microinjected in vero cells or in oocytes, respectively. Since L and NS proteins are essential for in vitro transcription by RNP, these results suggest that a trace amount of L protein may remain bound to the RNP and a host factor may stimulate residual L activity in vivo.

摘要

将水疱性口炎病毒纯化的具有转录活性的核糖核蛋白(RNP)复合物显微注射到非洲绿猴肾细胞中,可导致病毒的产生和释放。与在存在二乙氨基乙基葡聚糖的情况下用RNP处理的细胞释放病毒相比,显微注射技术效率很高。在非洲爪蟾卵母细胞中进行显微注射也导致感染的启动,如细胞质中病毒特异性蛋白的合成所示。进一步观察到,去除L蛋白但含有残留NS蛋白的RNP,分别显微注射到非洲绿猴肾细胞或卵母细胞中时,能够启动病毒产生或蛋白质合成。由于L蛋白和NS蛋白对于RNP的体外转录至关重要,这些结果表明,可能有微量的L蛋白仍与RNP结合,并且一种宿主因子可能在体内刺激残留的L蛋白活性。

相似文献

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Microinjection of vesicular stomatitis virus ribonucleoprotein into animal cells yields infectious virus.将水疱性口炎病毒核糖核蛋白显微注射到动物细胞中可产生有感染性的病毒。
Biochem Biophys Res Commun. 1983 Nov 15;116(3):1160-7. doi: 10.1016/s0006-291x(83)80264-2.
2
Specific interactions of vesicular stomatitis virus L and NS proteins with heterologous genome ribonucleoprotein template lead to mRNA synthesis in vitro.水泡性口炎病毒L蛋白和NS蛋白与异源基因组核糖核蛋白模板的特异性相互作用导致体外mRNA合成。
J Virol. 1984 Sep;51(3):628-34. doi: 10.1128/JVI.51.3.628-634.1984.
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Synthesis in vitro of full length genomic RNA and assembly of the nucleocapsid of vesicular stomatitis virus in a coupled transcription-translation system.在耦合转录-翻译系统中体外合成水疱性口炎病毒全长基因组RNA并组装核衣壳。
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Down-regulation of vesicular stomatitis virus transcription by the matrix protein of influenza virus.流感病毒基质蛋白对水疱性口炎病毒转录的下调作用。
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Dynamic Actin Filament Traps Mediate Active Diffusion of Vesicular Stomatitis Virus Ribonucleoproteins.动态肌动蛋白丝陷阱介导水疱性口炎病毒核糖核蛋白的活跃扩散。
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Purified matrix protein of vesicular stomatitis virus blocks viral transcription in vitro.水疱性口炎病毒的纯化基质蛋白在体外可阻断病毒转录。
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Requirements and functions of vesicular stomatitis virus L and NS proteins in the transcription process in vitro.水疱性口炎病毒L蛋白和NS蛋白在体外转录过程中的要求及功能
Biochem Biophys Res Commun. 1985 Jan 16;126(1):40-9. doi: 10.1016/0006-291x(85)90568-6.
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Expression and purification of vesicular stomatitis virus N-P complex from Escherichia coli: role in genome RNA transcription and replication in vitro.从大肠杆菌中表达和纯化水泡性口炎病毒N-P复合物:其在体外基因组RNA转录和复制中的作用
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In vitro phosphorylation of NS protein by the L protein of vesicular stomatitis virus.水泡性口炎病毒L蛋白对NS蛋白的体外磷酸化作用。
J Gen Virol. 1985 May;66 ( Pt 5):1025-36. doi: 10.1099/0022-1317-66-5-1025.
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Inhibition of transcription by immunoglobulins directed against the ribonucleoprotein of homotypic and heterotypic vesicular stomatitis viruses.针对同型和异型水疱性口炎病毒核糖核蛋白的免疫球蛋白对转录的抑制作用。
J Virol. 1978 Feb;25(2):675-84. doi: 10.1128/JVI.25.2.675-684.1978.

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PLoS One. 2012;7(4):e34623. doi: 10.1371/journal.pone.0034623. Epub 2012 Apr 2.
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Reviewing Chandipura: a vesiculovirus in human epidemics.审视钱迪普拉病毒:一种引发人类疫情的水疱性口炎病毒。
Biosci Rep. 2007 Oct;27(4-5):275-98. doi: 10.1007/s10540-007-9054-z.
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Specific interactions of vesicular stomatitis virus L and NS proteins with heterologous genome ribonucleoprotein template lead to mRNA synthesis in vitro.
水泡性口炎病毒L蛋白和NS蛋白与异源基因组核糖核蛋白模板的特异性相互作用导致体外mRNA合成。
J Virol. 1984 Sep;51(3):628-34. doi: 10.1128/JVI.51.3.628-634.1984.
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Transcription and replication of rhabdoviruses.弹状病毒的转录与复制
Microbiol Rev. 1987 Mar;51(1):66-87. doi: 10.1128/mr.51.1.66-87.1987.