A peptide based on the pore-forming domain of pro-apoptotic poliovirus 2B viroporin targets mitochondria
A peptide based on the pore-forming domain of pro-apoptotic poliovirus 2B viroporin targets mitochondria
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DOI：
10.1016/j.bbamem.2009.10.013
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发表时间：
2010-01-01
影响因子：
3.4
通讯作者：
Nieva, Jose L.
中科院分区：
文献类型：
--
作者：
Madan, Vanesa;Sanchez-Martinez, Silvia;Nieva, Jose L.
非结构性脊髓灰质炎病毒2B蛋白诱导质膜透化，最近被认为通过线粒体途径触发细胞凋亡。在这里，我们描述了成孔P3肽，基于2B两亲性结构域，易位通过培养细胞的质膜和目标线粒体。通过不同长度的P3版本的细胞透化，以及肽摄取分析支持依赖于P3与脂质双层物理相互作用并在其中建立渗透孔的能力的内化机制。内化的P3被发现与线粒体，但相反的父母2B蛋白，短肽不影响这些细胞器的形态或细胞分布，也不诱导细胞凋亡。我们的结论是，P3构成一个促凋亡序列，但缺乏2B促凋亡活性。(C)2009 Elsevier B.V.保留所有权利。
Non-structural poliovirus 2B protein induces plasma membrane permeabilization and has been recently implicated in triggering apoptosis via the mitochondrial pathway. Here we describe that the pore-forming P3 peptide, based on the 2B amphipathic domain, translocates through the plasma membrane of culture cells and targets mitochondria. Cell permeabilization by P3 versions of different lengths, together with peptide uptake analyses supported an internalization mechanism dependent on P3 capacity to interact physically with lipid bilayers and establish permeating pores therein. Internalized P3 was found associated with mitochondria, but contrary to the parental 2B protein, the short peptide did not affect the morphology or cell distribution of these organelles, nor induced apoptosis. We conclude that P3 constitutes a mitochondriotropic sequence, which is however devoid of 2B pro-apoptotic activity. (C) 2009 Elsevier B.V. All rights reserved.