细胞热休克蛋白 27 与经典猪瘟病毒 NS5A 蛋白相互作用，并通过 NF-κB 信号通路负调控病毒复制。
Cellular Hsp27 interacts with classical swine fever virus NS5A protein and negatively regulates viral replication by the NF-κB signaling pathway.
机构信息
Institute of Biotechnology, College of Life and Health Sciences, Northeastern University, No. 195, Chuangxin Road, Shenyang 110000, PR China.
Institute of Military Veterinary Medicine, Academy of Military Medical Sciences, No. 666 Liuying West Road, Changchun 130122, PR China.
出版信息
Virology. 2018 May;518:202-209. doi: 10.1016/j.virol.2018.02.020. Epub 2018 Mar 15.
Classical swine fever virus (CSFV) nonstructural protein NS5A is a multifunctional protein functioning in regulation of viral genome replication, protein translation and assembly by interaction with viral or host proteins. Here, heat shock protein 27 (Hsp27) has been identified as a novel binding partner of NS5A by using His tag "pull down" coupled with shotgun LC-MS/MS, with interaction of both proteins further confirmed by co-immunoprecipitation and laser confocal assays. In PK-15 cells, silencing of Hsp27 expression by siRNA enhanced CSFV replication, and upregulation of Hsp27 inhibited viral proliferation. Additionally, we have shown that overexpression of Hsp27 increased NF-κB signaling induced by TNFα. Blocking NF-κB signaling in PK-15 cells overexpressing Hsp27 by ammonium pyrrolidinedithiocarbamate (PDTC) eliminated the inhibition of CSFV replication by Hsp27. These findings clearly demonstrate that the inhibition of CSFV replication by Hsp27 is mediated via the NF-κB signaling pathway.
经典猪瘟病毒（CSFV）非结构蛋白 NS5A 是一种多功能蛋白，通过与病毒或宿主蛋白相互作用，在病毒基因组复制、蛋白翻译和组装的调节中发挥作用。本研究通过 His 标签“下拉”结合shotgun LC-MS/MS 鉴定热休克蛋白 27（Hsp27）为 NS5A 的一个新的结合伴侣，并用共免疫沉淀和激光共聚焦实验进一步证实了两者的相互作用。在 PK-15 细胞中，通过 siRNA 沉默 Hsp27 表达可增强 CSFV 复制，上调 Hsp27 抑制病毒增殖。此外，我们还表明，Hsp27 的过表达增加了 TNFα 诱导的 NF-κB 信号。用氨甲酰吡咯烷二硫代氨基甲酸盐（PDTC）阻断过表达 Hsp27 的 PK-15 细胞中的 NF-κB 信号通路可消除 Hsp27 对 CSFV 复制的抑制作用。这些发现清楚地表明，Hsp27 通过 NF-κB 信号通路抑制 CSFV 复制。
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