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裂谷热病毒G(N)糖蛋白的高尔基体保留基序的特征分析

Characterization of the Golgi retention motif of Rift Valley fever virus G(N) glycoprotein.

作者信息

Gerrard Sonja R, Nichol Stuart T

机构信息

Special Pathogens Branch, Division of Viral and Rickettsial Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30333, USA.

出版信息

J Virol. 2002 Dec;76(23):12200-10. doi: 10.1128/jvi.76.23.12200-12210.2002.

DOI:10.1128/jvi.76.23.12200-12210.2002
PMID:12414959
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC136907/
Abstract

As Rift Valley fever (RVF) virus, and probably all members of the family Bunyaviridae, matures in the Golgi apparatus, the targeting of the virus glycoproteins to the Golgi apparatus plays a pivotal role in the virus replication cycle. No consensus Golgi localization motif appears to be shared among the glycoproteins of these viruses. The viruses of the family Bunyaviridae synthesize their glycoproteins, G(N) and G(C), as a polyprotein. The Golgi localization signal of RVF virus has been shown to reside within the G(N) protein by use of a plasmid-based transient expression system to synthesize individual G(N) and G(C) proteins. While the distribution of individually expressed G(N) significantly overlaps with cellular Golgi proteins such as beta-COP and GS-28, G(C) expressed in the absence of G(N) localizes to the endoplasmic reticulum. Further analysis of expressed G(N) truncated proteins and green fluorescent protein/G(N) chimeric proteins demonstrated that the RVF virus Golgi localization signal mapped to a 48-amino-acid region of G(N) encompassing the 20-amino-acid transmembrane domain and the adjacent 28 amino acids of the cytosolic tail.

摘要

由于裂谷热(RVF)病毒,可能还有布尼亚病毒科的所有成员,都在高尔基体中成熟,因此病毒糖蛋白靶向高尔基体在病毒复制周期中起着关键作用。这些病毒的糖蛋白之间似乎没有共同的高尔基体定位基序。布尼亚病毒科的病毒将其糖蛋白G(N)和G(C)合成为一种多蛋白。通过使用基于质粒的瞬时表达系统来合成单个G(N)和G(C)蛋白,已证明RVF病毒的高尔基体定位信号位于G(N)蛋白内。虽然单独表达的G(N)的分布与细胞高尔基体蛋白如β-COP和GS-28有显著重叠,但在没有G(N)的情况下表达的G(C)定位于内质网。对表达的G(N)截短蛋白和绿色荧光蛋白/G(N)嵌合蛋白的进一步分析表明,RVF病毒高尔基体定位信号定位于G(N)的一个48个氨基酸的区域,该区域包括20个氨基酸的跨膜结构域和胞质尾的相邻28个氨基酸。

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