A peptide based on the pore-forming domain of pro-apoptotic poliovirus 2B viroporin targets mitochondria

作者：Madan Vanesa; Sanchez Martinez Silvia; Carrasco Luis; Nieva Jose L^*

来源：Biochimica et Biophysica Acta-Biomembranes, 2010, 1798(1): 52-58.

DOI：10.1016/j.bbamem.2009.10.013

• Enterovirus 2B
• Viroporin
• Protein-lipid interaction
• Pore-forming peptide
• Viral protein-induced apoptosis

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.

• 出版日期2010-1