Department of Biological Sciences, University at Albany, Albany, NY, 12222, USA.
Department of Biological Sciences, University at Albany, Albany, NY, 12222, USA; The RNA Institute, University at Albany, NY, 12222, USA.
Virology. 2020 Jun;545:53-62. doi: 10.1016/j.virol.2020.03.004. Epub 2020 Mar 25.
Viruses have evolved strategies to ensure efficient translation using host cell ribosomes and translation factors. In addition to cleaving translation initiation factors required for host cell translation, poliovirus (PV) uses an internal ribosome entry site (IRES). Recent studies suggest that viruses exploit specific ribosomal proteins to enhance translation of their viral proteins. The ribosomal protein receptor for activated C kinase 1 (RACK1), a protein of the 40S ribosomal subunit, was previously shown to mediate translation from the 5' cricket paralysis virus and hepatitis C virus IRESs. Here we found that translation of a PV dual-luciferase reporter shows a moderate dependence on RACK1. However, in the context of a viral infection we observed significantly reduced poliovirus plaque size and titers and delayed host cell translational shut-off. Our findings further illustrate the involvement of the cellular translational machinery during PV infection and how viruses usurp the function of specific ribosomal proteins.
病毒已经进化出了利用宿主细胞核糖体和翻译因子来确保高效翻译的策略。除了切割宿主细胞翻译所需的翻译起始因子外,脊髓灰质炎病毒(PV)还使用内部核糖体进入位点(IRES)。最近的研究表明,病毒利用特定的核糖体蛋白来增强其病毒蛋白的翻译。核糖体蛋白激活 C 激酶 1(RACK1)受体是 40S 核糖体亚基的一种蛋白质,先前已被证明可介导来自 5'蟋蟀麻痹病毒和丙型肝炎病毒 IRES 的翻译。在这里,我们发现 PV 双荧光素酶报告基因的翻译适度依赖于 RACK1。然而,在病毒感染的情况下,我们观察到 PV 蚀斑大小和滴度显著降低,以及宿主细胞翻译关闭延迟。我们的发现进一步说明了细胞翻译机制在 PV 感染过程中的参与情况,以及病毒如何篡夺特定核糖体蛋白的功能。