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N-糖基化蛋白对博尔纳病病毒（BDV）的感染性很重要。

N-glycosylated protein(s) are important for the infectivity of Borna disease virus (BDV).

作者信息

Stoyloff R, Briese T, Borchers K, Zimmermann W, Ludwig H

机构信息

Institut für Virologie, Freie Universität Berlin, Federal Republic of Germany.

出版信息

Arch Virol. 1994;137(3-4):405-9. doi: 10.1007/BF01309486.

DOI:10.1007/BF01309486
PMID:7944960
Abstract

Tunicamycin inhibited the production of infectious Borna disease virus (BDV) and glycosidase treatment eliminated the infectivity of cell-free virus. A glycoprotein of approximately 17 kDa, found in association with infectious virus, was identified by Concanavalin A binding.

摘要

衣霉素抑制传染性博尔纳病病毒（BDV）的产生，糖苷酶处理可消除无细胞病毒的感染性。通过伴刀豆球蛋白A结合鉴定出一种与传染性病毒相关的约17 kDa的糖蛋白。

相似文献

1
N-glycosylated protein(s) are important for the infectivity of Borna disease virus (BDV).N-糖基化蛋白对博尔纳病病毒（BDV）的感染性很重要。
Arch Virol. 1994;137(3-4):405-9. doi: 10.1007/BF01309486.
2
N-terminal domain of Borna disease virus G (p56) protein is sufficient for virus receptor recognition and cell entry.博尔纳病病毒G（p56）蛋白的N端结构域足以识别病毒受体并介导细胞进入。
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Cell entry of Borna disease virus follows a clathrin-mediated endocytosis pathway that requires Rab5 and microtubules.博尔纳病病毒的细胞进入遵循网格蛋白介导的内吞途径，该途径需要Rab5和微管。
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Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface.分子伴侣BiP在细胞表面与博尔纳病病毒糖蛋白相互作用。
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The glycosylated matrix protein of Borna disease virus is a tetrameric membrane-bound viral component essential for infection.博尔纳病病毒的糖基化基质蛋白是一种四聚体膜结合病毒成分，对感染至关重要。
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Borna disease virus glycoprotein is required for viral dissemination in neurons.博尔纳病病毒糖蛋白是病毒在神经元中传播所必需的。
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Persistent human Borna disease virus infection modifies the acetylome of human oligodendroglia cells towards higher energy and transporter levels.持续性人博尔纳病病毒感染使人类少突胶质细胞的乙酰化蛋白质组向更高的能量和转运体水平转变。
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Biochemical and functional analysis of the Borna disease virus G protein.博尔纳病病毒G蛋白的生化与功能分析
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Modulation of miR-122 on persistently Borna disease virus infected human oligodendroglial cells.调节 miR-122 对持续感染博尔纳病病毒的人少突胶质细胞的影响。
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引用本文的文献

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Open reading frame III of borna disease virus encodes a nonglycosylated matrix protein.

本文引用的文献

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Biology and neurobiology of Borna disease viruses (BDV), defined by antibodies, neutralizability and their pathogenic potential.
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Genomic organization of Borna disease virus.博尔纳病病毒的基因组结构
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Enzymatic deglycosylation of asparagine-linked glycans: purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum.天冬酰胺连接聚糖的酶促去糖基化作用：脑膜炎败血金黄杆菌中寡糖裂解酶的纯化、性质及特异性
博尔纳病病毒的开放阅读框III编码一种非糖基化的基质蛋白。
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Borna disease virus.博尔纳病病毒
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Biochemical and functional analysis of the Borna disease virus G protein.博尔纳病病毒G蛋白的生化与功能分析
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Neutralizing antibodies in Borna disease virus-infected rats.博尔纳病病毒感染大鼠体内的中和抗体
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Borna disease virus (BDV), a nonsegmented RNA virus, replicates in the nuclei of infected cells where infectious BDV ribonucleoproteins are present.博尔纳病病毒（BDV）是一种不分节段的RNA病毒，在被感染细胞的细胞核中复制，细胞核中存在具有感染性的BDV核糖核蛋白。
J Virol. 1994 Mar;68(3):1371-81. doi: 10.1128/JVI.68.3.1371-1381.1994.
5
Sequence and genome organization of Borna disease virus.博尔纳病病毒的序列与基因组结构
J Virol. 1994 Mar;68(3):1382-96. doi: 10.1128/JVI.68.3.1382-1396.1994.
6
A novel marker for Borna disease virus infection.博尔纳病病毒感染的一种新型标志物。
Lancet. 1994 Jan 29;343(8892):297-8. doi: 10.1016/s0140-6736(94)91147-9.
7
Optimizing hydrolysis of N-linked high-mannose oligosaccharides by endo-beta-N-acetylglucosaminidase H.通过内切-β-N-乙酰氨基葡萄糖苷酶H优化N-连接的高甘露糖寡糖的水解作用。
Anal Biochem. 1984 Sep;141(2):515-22. doi: 10.1016/0003-2697(84)90080-0.
8
Isolation and characterization of a 14500 molecular weight protein from brains and tissue cultures persistently infected with borna disease virus.从持续感染博尔纳病病毒的大脑和组织培养物中分离并鉴定一种分子量为14500的蛋白质。
J Gen Virol. 1985 Nov;66 ( Pt 11):2479-84. doi: 10.1099/0022-1317-66-11-2479.
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Increase of virus yields and releases of Borna disease virus from persistently infected cells.持续性感染细胞中博尔纳病病毒的病毒产量增加及释放
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Purification and properties of an intranuclear virus-specific antigen from tissue infected with Borna disease virus.从感染博尔纳病病毒的组织中纯化核内病毒特异性抗原及其特性
J Gen Virol. 1986 Feb;67 ( Pt 2):235-41. doi: 10.1099/0022-1317-67-2-235.