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本文引用的文献

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Flaviviruses: braking the entering.黄病毒:阻断进入。
Curr Opin Virol. 2013 Feb;3(1):3-12. doi: 10.1016/j.coviro.2012.12.001. Epub 2013 Jan 24.
2
Cryo-EM structure of the mature dengue virus at 3.5-Å resolution.成熟登革热病毒的 3.5Å 分辨率冷冻电镜结构。
Nat Struct Mol Biol. 2013 Jan;20(1):105-10. doi: 10.1038/nsmb.2463. Epub 2012 Dec 16.
3
Structure of a dengue virus envelope protein late-stage fusion intermediate.登革病毒包膜蛋白晚期融合中间态结构。
J Virol. 2013 Feb;87(4):2287-93. doi: 10.1128/JVI.02957-12. Epub 2012 Dec 12.
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Flavivirus cell entry and membrane fusion.黄病毒的细胞进入和膜融合。
Viruses. 2011 Feb;3(2):160-171. doi: 10.3390/v3020160. Epub 2011 Feb 22.
5
Mutational analysis of the zippering reaction during flavivirus membrane fusion.在黄病毒膜融合过程中 zippering 反应的突变分析。
J Virol. 2011 Sep;85(17):8495-501. doi: 10.1128/JVI.05129-11. Epub 2011 Jun 22.
6
Immunodominance and functional activities of antibody responses to inactivated West Nile virus and recombinant subunit vaccines in mice.免疫优势与抗体对灭活西尼罗河病毒和重组亚单位疫苗反应的功能活性在小鼠中的研究。
J Virol. 2011 Mar;85(5):1994-2003. doi: 10.1128/JVI.01886-10. Epub 2010 Dec 8.
7
Peptide inhibitors of flavivirus entry derived from the E protein stem.来源于 E 蛋白茎的黄病毒进入抑制剂肽。
J Virol. 2010 Dec;84(24):12549-54. doi: 10.1128/JVI.01440-10. Epub 2010 Sep 29.
8
Molecular mechanisms involved in the early steps of flavivirus cell entry.参与黄病毒细胞进入早期步骤的分子机制。
Microbes Infect. 2011 Jan;13(1):1-9. doi: 10.1016/j.micinf.2010.09.005. Epub 2010 Dec 10.
9
Peptide inhibitors of dengue-virus entry target a late-stage fusion intermediate.登革热病毒进入抑制剂针对晚期融合中间态。
PLoS Pathog. 2010 Apr 8;6(4):e1000851. doi: 10.1371/journal.ppat.1000851.
10
In vitro reconstitution reveals key intermediate states of trimer formation by the dengue virus membrane fusion protein.体外重建揭示了登革热病毒膜融合蛋白三聚体形成的关键中间状态。
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膜近端“茎”区增加了黄病毒 E 蛋白融合后三聚体的稳定性,并调节其结构。

The membrane-proximal "stem" region increases the stability of the flavivirus E protein postfusion trimer and modulates its structure.

机构信息

Department of Virology, Medical University of Vienna, Vienna, Austria.

出版信息

J Virol. 2013 Sep;87(17):9933-8. doi: 10.1128/JVI.01283-13. Epub 2013 Jun 26.

DOI:10.1128/JVI.01283-13
PMID:23804648
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3754098/
Abstract

The flavivirus fusion protein E contains a "stem" region which is hypothesized to be crucial for driving fusion. This sequence element connects the ectodomain to the membrane anchor, and its structure in the trimeric postfusion conformation is still poorly defined. Using E trimers of tick-borne encephalitis virus with stem truncations of different lengths, we show that the N-terminal part of the stem increases trimer stability and also modulates the trimer structure outside the stem interaction site.

摘要

黄病毒融合蛋白 E 包含一个“茎”区,该区域被假设对于驱动融合至关重要。该序列元件将外域连接到膜锚定,但其在三聚体融合构象中的结构仍未得到很好的定义。使用具有不同长度茎截断的蜱传脑炎病毒 E 三聚体,我们表明茎的 N 端部分增加了三聚体稳定性,并且还调节了茎相互作用位点之外的三聚体结构。