Garcel A, Gout E, Timmins J, Chroboczek J, Fender P
Institut de Biologie Structurale, 41 rue Jules Horowitz, 38027 Grenoble, France.
J Gene Med. 2006 Apr;8(4):524-31. doi: 10.1002/jgm.862.
Direct protein transduction is a recent technique that involves use of peptide vectors. In this study, we demonstrate that adenovirus dodecahedron (Dd), a virus-like particle devoid of DNA and able to penetrate cells with high efficiency, can be used as a vector for protein delivery.
Taking advantage of Dd interaction with structural domains called WW, we have elaborated a universal adaptor to attach a protein of interest to this vector.
A tandem of three WW structural domains derived from the Nedd4 protein enables the formation of stable complexes with Dd, without impairing its endocytosis efficiency. Our protein of interest fused to the triple WW linker is delivered by the dodecahedron in 100% of cells in culture with on average more than ten million molecules per cell.
These data demonstrate the great potential of adenovirus dodecahedron in combination with WW domains as a protein transduction vector.
直接蛋白质转导是一项涉及使用肽载体的新技术。在本研究中，我们证明了腺病毒十二面体（Dd），一种不含DNA且能高效穿透细胞的病毒样颗粒，可作为蛋白质递送载体。
利用Dd与称为WW的结构域的相互作用，我们构建了一种通用接头，将感兴趣的蛋白质连接到该载体上。
源自Nedd4蛋白的三个WW结构域串联体能够与Dd形成稳定复合物，而不损害其胞吞效率。与三联WW接头融合的我们感兴趣的蛋白质，由十二面体递送至培养物中100%的细胞，平均每个细胞超过一千万个分子。
这些数据证明了腺病毒十二面体与WW结构域结合作为蛋白质转导载体的巨大潜力。
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