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首页> 外文期刊>Journal of Molecular Biochemistry >Study on the internalization mechanism of the ZEBRA cell-penetrating peptide
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Study on the internalization mechanism of the ZEBRA cell-penetrating peptide

机译：ZEBRA细胞穿透肽的内在化机理研究

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Cell-penetrating peptides (CPPs) represent a noninvasive method for delivering functional biomolecules into living cells. We have recently shown that the Epstein-Barr virus transcriptional factor ZEBRA contains a protein transduction domain, named Z9 or minimal domain (MD). Only few of currently identified CPPs including MD are able to rapidly cross the mammalian cell membrane without being entrapped into endosomal compartments, even when fused to cargo macromolecules. In this work, a series of MD deletion mutants has been engineered and their cellular uptake has been analyzed by confocal microscopy and FACS. We identified a domain MD 11 (8 amino acids shorter than MD) able to enter mammalian cells via a mainly endocytosis-independent mechanism. All the other generated truncated forms exhibited reduced cellular uptake and penetrated into cells through endocytic mechanisms. These results have highlighted the role of the MD 11 C-terminal region as essential for efficient cellular entry and endosomal escape? and open new perspectives for the use of this CPP as carrier for delivering biologically active macromolecules with therapeutic potential.
机译：细胞穿透肽（CPP）代表了一种将功能性生物分子传递到活细胞中的非侵入性方法。我们最近显示，爱泼斯坦-巴尔病毒转录因子ZEBRA包含一个蛋白质转导结构域，称为Z9或最小结构域（MD）。包括MD在内的目前鉴定出的CPP中，只有极少数能够快速穿越哺乳动物细胞膜而不会陷入内体区室，即使与货物大分子融合也是如此。在这项工作中，已经设计了一系列的MD缺失突变体，并通过共聚焦显微镜和FACS分析了它们的细胞摄取。我们确定了域MD 11（比MD短8个氨基酸）能够通过主要的内吞不依赖机制进入哺乳动物细胞。所有其他产生的截短形式表现出减少的细胞摄取并通过内吞机制渗透到细胞中。这些结果突出了MD 11 C末端区域对于有效进入细胞和内体逃逸至关重要的作用。并为使用这种CPP作为载体提供具有治疗潜力的生物活性大分子开辟了新的前景。

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