Zhang Wei, Arcos Rebecca
Department of Pharmacology, University of Texas Health Science Center, San Antonio, TX 78229-3900, USA.
Virology. 2005 Apr 10;334(2):194-202. doi: 10.1016/j.virol.2005.01.048.
Adenovirus is one of the well-studied double-stranded DNA viruses. However, the mechanisms of its DNA packaging and virion assembly are still not fully understood. One of the unique features of adenovirus is that the unpackaged viral DNA is associated with core protein pVII. Packaging of viral DNA bound with proteins has not been reported from other viruses. To characterize how viral DNA bound with protein pVII is packaged, we performed experiments to see if protein pVII interacts with the known DNA packaging proteins or the packaging sequence. Our results demonstrated that protein pVII interacted with the viral IVa2 and L1 52/55 kDa proteins, which are the known viral DNA packaging proteins. Furthermore, our protein-DNA binding experiments demonstrated that the IVa2 protein mediates the specific interaction with the packaging sequence, whereas protein pVII and the L1 52/55 kDa protein bind to DNA non-specifically. Although the non-specific binding of protein pVII and the L1 52/55 kDa protein do not appear to affect the specific binding of the IVa2 protein to the packaging sequence, and the specific binding of the IVa2 protein does not appear to block the bindings of protein pVII and the L1 52/55 kDa protein to the packaging sequence, the possibility of a cooperative binding among the IVa2 protein, the L1 52/55 kDa protein and protein pVII on the packaging sequence needs to be further determined. In summary, the results indicate that the assembly of the DNA packaging initiation complex may be mediated by the specific interaction of the IVa2 protein with the packaging sequence and other viral proteins, such as protein pVII and the L1 52/55 kDa protein.
腺病毒是一种经过充分研究的双链DNA病毒。然而,其DNA包装和病毒体组装的机制仍未完全了解。腺病毒的一个独特特征是未包装的病毒DNA与核心蛋白pVII相关联。其他病毒尚未报道过与蛋白质结合的病毒DNA的包装情况。为了表征与蛋白pVII结合的病毒DNA是如何被包装的,我们进行了实验,以观察蛋白pVII是否与已知的DNA包装蛋白或包装序列相互作用。我们的结果表明,蛋白pVII与病毒IVa2和L1 52/55 kDa蛋白相互作用,这两种蛋白是已知的病毒DNA包装蛋白。此外,我们的蛋白质-DNA结合实验表明,IVa2蛋白介导与包装序列的特异性相互作用,而蛋白pVII和L1 52/55 kDa蛋白则非特异性地结合到DNA上。尽管蛋白pVII和L1 52/55 kDa蛋白的非特异性结合似乎不影响IVa2蛋白与包装序列的特异性结合,并且IVa2蛋白的特异性结合似乎也不阻止蛋白pVII和L1 52/55 kDa蛋白与包装序列的结合,但IVa2蛋白、L1 52/55 kDa蛋白和蛋白pVII在包装序列上协同结合的可能性仍需进一步确定。总之,结果表明DNA包装起始复合物的组装可能是由IVa2蛋白与包装序列以及其他病毒蛋白(如蛋白pVII和L1 52/55 kDa蛋白)的特异性相互作用介导的。