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首页> 外文期刊>Journal of Molecular Biology >Plasma membrane-porating domain in poliovirus 2B protein. A short peptide mimics viroporin activity.
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Plasma membrane-porating domain in poliovirus 2B protein. A short peptide mimics viroporin activity.

机译：脊髓灰质炎病毒2B蛋白中的质膜穿孔结构域。短肽模拟维罗帕林活性。

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Picornavirus 2B, a non-structural protein required for effective viral replication, has been implicated in cell membrane permeabilization during the late phases of infection. Here, we have approached the molecular mechanism of this process by assessing the pore-forming activity of an overlapping peptide library that spanned the complete 2B sequence. At non-cytopathic concentrations, only the P3 peptide, spanning 2B residues 35-55, effectively assembled hydrophilic pores that allowed diffusion of low molecular mass solutes across the cell plasma membrane (IC(50) approximately 4x10(-7) M) and boundary liposome bilayers (starting at peptide to lipid molar ratios>1:10(4)). Circular dichroism data were consistent with its capacity to fold as a helix in a membrane-like environment. Furthermore, addition of this peptide to a sealed plasma-membrane model, consisting of retinal rod outer segments patch-clamped in a whole-cell configuration, induced ion channel activity within seconds at concentrations as low as10(-8) M. Thus, we have established a "one-helix" 2B version that possesses the intrinsic pore-forming activity required to directly and effectively permeabilize the cell plasma membrane. We conclude that 2B viroporin can be classified as a genuine pore-forming toxin of viral origin, which is produced intracellularly at certain times post infection.
机译：有效感染病毒复制所必需的非结构蛋白小核糖核酸病毒2B，已在感染后期与细胞膜通透性有关。在这里，我们已经通过评估覆盖整个2B序列的重叠肽库的成孔活性来探讨了该过程的分子机制。在非细胞病变浓度下，只有跨越2B残基35-55的P3肽才能有效组装亲水孔，从而允许低分子量溶质在细胞质膜（IC（50）约4x10（-7）M）和边界上扩散脂质体双层（从肽与脂质的摩尔比> 1:10（4）开始）。圆二色性数据与其在膜状环境中折叠成螺旋状的能力是一致的。此外，将此肽添加到一个密封的血浆膜模型中，该模型由以全细胞配置补丁固定的视网膜棒外段组成，可在几秒钟内在低至10（-8）M的浓度下诱导离子通道活性。因此，我们已经建立了一种“单螺旋” 2B型，该型具有直接有效地透化细胞质膜所需的固有成孔活性。我们得出的结论是2B viroporin可以归类为病毒来源的真正的成孔毒素，它是在感染后的某些时间在细胞内产生的。

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