在8.8 Å分辨率的完整病毒颗粒中,未成熟的HIV-1囊体的结构
Florian K M Schur1, Wim J H Hagen2, Michaela Rumlová3
11] Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany [2] Molecular Medicine Partnership Unit, European Molecular Biology Laboratory/Universitätsklinikum Heidelberg, Heidelberg, Germany.
Nature
|November 4, 2014
概括
研究人员可视化了人类免疫缺陷病毒1型 (HIV-1) 体格子结构. 这揭示了与以前的模型不同的新型组装相互作用,进步了我们对逆转录病毒组装的理解.
科学领域:
- 结构生物学是结构生物学.
- 病毒学 病毒学
- 生物物理学的生物物理.
背景情况:
- 人类免疫缺陷病毒1型 (HIV-1) 组装涉及Gag多蛋白格子的形成和蛋白酶裂变.
- 不同质的颗粒大小和形态学阻碍了对逆转病毒的高分辨率结构分析.
- 现有的Gag蛋白相互作用模型是基于相关病毒的体外研究.
研究的目的:
- 在亚纳米分辨率下确定未成熟的HIV-1体网格的in situ结构.
- 确定介导HIV-1组装的三级和四级结构相互作用.
- 将HIV-1囊组合与其他逆转录病毒的组合进行比较.
主要方法:
- 低温电子断层扫描用于成像完整的未成熟的HIV-1颗粒.
- 应用了子断层图像平均方法来解决体晶格结构.
- 为了进行比较,我们还确定了梅森-瑞子病毒囊网格的结构.
主要成果:
- 未成熟的HIV-1的体格子结构在亚纳米分辨率下得到解析,使得精确的α-螺旋定位成为可能.
- 揭示了控制HIV-1组装的新型三级和四级结构相互作用.
- 与Mason-Pfizer子病毒的比较显示,在组装过程中,逆转录病毒囊蛋白中保留了三级结构,但有不同的四级安排.
结论:
- 这项研究提供了未成熟的HIV-1囊的高分辨率结构模型.
- 逆转录病毒囊蛋白在组装过程中表现出明显的四级排列,尽管保留了三级结构.
- 低温电子断层扫描方法对于在异质生物环境中研究蛋白质结构非常有价值.
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