International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
J Gen Virol. 2010 Jun;91(Pt 6):1478-83. doi: 10.1099/vir.0.019794-0. Epub 2010 Feb 17.
When Ebola virus nucleoprotein (NP) is expressed in mammalian cells, it assembles into helical structures. Here, the recombinant NP helix purified from cells expressing NP was characterized biochemically and morphologically. We found that the recombinant NP helix is associated with non-viral RNA, which is not protected from RNase digestion and that the morphology of the helix changes depending on the environmental salt concentration. The N-terminal 450 aa residues of NP are sufficient for these properties. However, digestion of the NP-associated RNA eliminates the plasticity of the helix, suggesting that this RNA is an essential structural component of the helix, binding to individual NP molecules via the N-terminal 450 aa. These findings enhance our knowledge of Ebola virus assembly and understanding of the Ebola virus life cycle.
当埃博拉病毒核蛋白（NP）在哺乳动物细胞中表达时，它会组装成螺旋结构。在这里，从表达 NP 的细胞中纯化的重组 NP 螺旋通过生化和形态学进行了表征。我们发现，从重组 NP 螺旋中分离出的非病毒 RNA 与螺旋相关联，该 RNA 不能免受 RNase 消化，并且螺旋的形态取决于环境盐浓度而变化。NP 的 N 端 450 个残基足以具有这些性质。但是，NP 相关 RNA 的消化消除了螺旋的可塑性，这表明该 RNA 是螺旋的必需结构成分，通过 N 端 450 个残基与单个 NP 分子结合。这些发现增进了我们对埃博拉病毒组装的认识，并加深了对埃博拉病毒生命周期的理解。
