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首页> 外文期刊>Biochemistry >Dynamics of Zika Virus Capsid Protein in Solution: The Properties and Exposure of the Hydrophobic Cleft Are Controlled by the alpha-Helix 1 Sequence
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Dynamics of Zika Virus Capsid Protein in Solution: The Properties and Exposure of the Hydrophobic Cleft Are Controlled by the alpha-Helix 1 Sequence

机译：溶液中Zika病毒衣壳蛋白的动态：疏水性裂缝的性质和暴露由α-螺旋1序列控制

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Zika virus (ZIKV) became an important public health concern because infection was correlated to the development of microcephaly and other neurological disorders. Although the structure of the virion has been determined by cryo-electron microscopy, information about the nucleocapsid is lacking. We used nuclear magnetic resonance to determine the solution structure and dynamics of full length ZIKV capsid protein (ZIKVC). Although most of the protein is structured as described for the capsid proteins of Dengue and West Nile viruses and for truncated ZIKVC (residues 23-98), here we show important differences in the alpha-helix 1 and N-terminal intrinsically disordered region (IDR). We distinguished two dynamical regions in the ZIKVC IDR, a highly flexible N-terminal end and a transitional disordered region, indicating that it contains ordered segments rather than being completely flexible. The unique size and orientation of alpha-helix 1 partially occlude the protein hydrophobic cleft. Measurements of the dynamics of alpha-helix 1, surface exposure, and thermal susceptibility of each backbone amide H-1 in protein structure revealed the occlusion of the hydrophobic cleft by alpha 1/alpha 1' and supported alpha-helix 1 positional uncertainty. On the basis of the findings described here, we propose that the dynamics of ZIKVC structural elements responds to a structure-driven regulation of interaction of the protein with intracellular hydrophobic interfaces, which would have an impact on the switches that are necessary for nucleocapsid assembly. Subtle differences in the sequence of alpha-helix 1 have an impact on its size and orientation and on the degree of exposure of the hydrophobic cleft, suggesting that alpha-helix 1 is a hot spot for evolutionary adaptation of the capsid proteins of flaviviruses.
机译：Zika病毒（ZIKV）成为一个重要的公共卫生问题，因为感染与微微术和其他神经疾病的发育相关。虽然Viriv的结构已经通过冷冻电子显微镜确定，但是缺乏关于核衣壳的信息。我们使用核磁共振来确定全长ZIKV胶囊蛋白（ZIKVC）的解决方案结构和动力学。虽然大多数蛋白质被描述为Dengue和West Nile病毒的衣壳蛋白和截短的Zikvc（残留物23-98）所述，但在这里，我们展示了α-螺旋1和N末端内部无序区域的重要差异（IDR ）。我们在ZIKVC IDR中分别了两个动态区域，高度柔性的N末端和过渡无序区域，表明它包含有序的段而不是完全柔性。 α-螺旋1的独特尺寸和取向部分闭塞蛋白质疏水性裂缝。 α-螺旋1，表面暴露和蛋白质结构中每个骨干酰胺H-1的动力学的测量揭示了α1/α1'和支持的α-螺旋1位置不确定度的疏水裂缝的闭塞。在这里描述的结果的基础上，我们提出了Zikvc结构元件的动态对蛋白质与细胞内疏水界面的相互作用的结构驱动的调节，这会对核衣壳组件所需的开关产生影响。 α-螺旋1序列中的微妙差异对其尺寸和方向和疏水性裂缝的暴露程度产生影响，表明α-螺旋1是对黄病毒囊体蛋白的进化适应的热点。

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  • 来源
    《Biochemistry》 |2019年第20期|共11页
  • 作者

    Morando Maria A.; Barbosa Glauce M.; Cruz-Oliveira Christine; Da Poian Andrea T.; Almeida Fabio C. L.;

  • 作者单位

    Univ Fed Rio de Janeiro Program Struct Biol Inst Med Biochem Leopoldo De Meis BR-21941902 Rio De Janeiro Brazil;

    Univ Fed Rio de Janeiro Program Struct Biol Inst Med Biochem Leopoldo De Meis BR-21941902 Rio De Janeiro Brazil;

    Univ Fed Rio de Janeiro Program Struct Biol Inst Med Biochem Leopoldo De Meis BR-21941902 Rio De Janeiro Brazil;

    Univ Fed Rio de Janeiro Program Struct Biol Inst Med Biochem Leopoldo De Meis BR-21941902 Rio De Janeiro Brazil;

    Univ Fed Rio de Janeiro Program Struct Biol Inst Med Biochem Leopoldo De Meis BR-21941902 Rio De Janeiro Brazil;

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  • 中图分类 生物化学;
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