Schoggins John W, Falck-Pedersen Erik
Weill Medical College of Cornell University, Hearst Research Foundation, Department of Microbiology and Immunology, Molecular Biology Graduate Program, 1300 York Avenue, New York, NY 10021, USA.
Virology. 2009 Dec 5;395(1):10-20. doi: 10.1016/j.virol.2009.08.041. Epub 2009 Sep 25.
Adenovirus is a well-established viral gene transfer model system that presents two major hurdles when being considered for cell-specific targeting applications. First is the need to detarget the vector from inherent host binding mechanisms, and second is the need to establish a productive and stable method to retarget the vector to a desired cell receptor. In previous studies we had generated an adenovirus vector platform that lacks the normal targeting attributes derived from the fiber and penton capsid proteins. In the current study we characterized our detargeted Ad5-based vectors (Ad5.F7F41S and Ad5.F7F41SDeltaRGD) as platforms for novel retargeted viruses. The experimental strategy relied on incorporating small peptide ligands into several sites of the Ad 41short fiber knob domain (AB, CD, HI, G and Cterm). Reengineering of Ad41 short fiber resulted either in a bypass to fiber 7 usage, or in a dominant negative packaging/production deficiency phenotype. Under specific growth conditions we could remedy some of the capsid deficiencies and generate high titer viruses. However when examined by Western blot analysis, the resulting viruses were still defective in capsid content. The tandem fiber F7F41S platform has revealed an unanticipated sensitivity of Adenovirus packaging to fiber 41short structural modifications. These studies indicate fiber assembly into an intact virion or fiber influenced capsid stability as a bottleneck to efficient particle production. We also demonstrate that virus particles characterized as mature virions following CsCl banding can vary significantly in capsid protein content. Considering the complexity of virus entry into a target cell, modified "mature virions" may be compromised at the level of transduction not only through the intended modification, but also by virtue of secondary structural packaging conflicts.
腺病毒是一种成熟的病毒基因转移模型系统,在考虑用于细胞特异性靶向应用时存在两个主要障碍。首先,需要使载体避开固有的宿主结合机制,其次,需要建立一种有效且稳定的方法,将载体重新靶向到所需的细胞受体。在先前的研究中,我们构建了一个腺病毒载体平台,该平台缺乏源自纤维和五聚体衣壳蛋白的正常靶向属性。在当前的研究中,我们将基于Ad5的去靶向载体(Ad5.F7F41S和Ad5.F7F41SDeltaRGD)表征为新型重新靶向病毒的平台。实验策略依赖于将小肽配体掺入Ad 41短纤维钮结构域的几个位点(AB、CD、HI、G和C末端)。Ad41短纤维的重新设计要么导致绕过纤维7的使用,要么导致显性负性包装/生产缺陷表型。在特定的生长条件下,我们可以弥补一些衣壳缺陷并产生高滴度病毒。然而,通过蛋白质免疫印迹分析检测时,产生的病毒在衣壳含量上仍然存在缺陷。串联纤维F7F41S平台揭示了腺病毒包装对纤维41短结构修饰的意外敏感性。这些研究表明,纤维组装成完整的病毒粒子或纤维对衣壳稳定性的影响是高效产生病毒粒子的一个瓶颈。我们还证明,经CsCl梯度离心后表征为成熟病毒粒子的病毒粒子在衣壳蛋白含量上可能有显著差异。考虑到病毒进入靶细胞的复杂性,修饰后的“成熟病毒粒子”不仅可能因预期的修饰而在转导水平上受损,还可能由于二级结构包装冲突而受损。