School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
FEBS Lett. 2013 Jul 11;587(14):2118-24. doi: 10.1016/j.febslet.2013.05.029. Epub 2013 May 28.
Although non-structural protein 1 (NS1) of influenza viruses is not essential for virulence, this protein is involved in host-virus interactions, viral replication, and translation. In particular, NS1 is known to interact with the host protein, staufen1 (Stau1). This interaction is important for efficient viral replication. However, the underlying molecular mechanism by which NS1 influences the viral life cycle remains obscure. Here, we show using immunoprecipitation and artificial tethering that the N-terminus of NS1, NS1(1-73), interacts with Stau1, blocks the Stau1-Upf1 interaction, and consequently inhibits the efficiency of Stau1-mediated mRNA decay (SMD), but not nonsense-mediatedmRNA decay (NMD). The regulation of SMD efficiency by NS1 may contribute to building a more favorable cellular environment for viral replication.
虽然流感病毒的非结构蛋白 1（NS1）对于毒力不是必需的，但这种蛋白参与宿主-病毒相互作用、病毒复制和翻译。特别是，NS1 已知与宿主蛋白 staufen1（Stau1）相互作用。这种相互作用对于有效的病毒复制很重要。然而，NS1 影响病毒生命周期的潜在分子机制仍然不清楚。在这里，我们通过免疫沉淀和人工连接显示，NS1 的 N 端，NS1（1-73），与 Stau1 相互作用，阻断 Stau1-Upf1 相互作用，从而抑制 Stau1 介导的 mRNA 衰减（SMD）的效率，但不抑制无意义介导的 mRNA 衰减（NMD）。NS1 对 SMD 效率的调节可能有助于为病毒复制建立更有利的细胞环境。
