Institute of Virology and AIDS Research, The First Hospital of Jilin University, Changchun, Jilin, China.
Research Unit of Key Technologies for Prevention and Control of Virus Zoonoses, Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Changchun, Jilin, China.
mBio. 2024 Feb 14;15(2):e0307123. doi: 10.1128/mbio.03071-23. Epub 2024 Jan 24.
The accessory protein ORF6 of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a key interferon (IFN) antagonist that strongly suppresses the production of primary IFN as well as the expression of IFN-stimulated genes. However, how host cells respond to ORF6 remains largely unknown. Our research of ORF6-binding proteins by pulldown revealed that E3 ligase components such as Cullin 4B (CUL4B), DDB1, and RBX1 are potential ORF6-interacting proteins. Further study found that the substrate recognition receptor PRPF19 interacts with CUL4B, DDB1, and RBX1 to form a CRL4B-based E3 ligase, which catalyzes ORF6 ubiquitination and subsequent degradation. Overexpression of PRPF19 promotes ORF6 degradation, releasing ORF6-mediated IFN inhibition, which inhibits SARS-CoV-2 replication. Moreover, we found that activation of CUL4B by the neddylation inducer etoposide alleviates lung lesions in a SARS-CoV-2 mouse infection model. Therefore, targeting ORF6 for degradation may be an effective therapeutic strategy against SARS-CoV-2 infection.IMPORTANCEThe cellular biological function of the ubiquitin-proteasome pathway as an important modulator for the regulation of many fundamental cellular processes has been greatly appreciated. The critical role of the ubiquitin-proteasome pathway in viral pathogenesis has become increasingly apparent. It is a powerful tool that host cells use to defend against viral infection. Some cellular proteins can function as restriction factors to limit viral infection by ubiquitin-dependent degradation. In this research, we identificated of CUL4B-DDB1-PRPF19 E3 Ubiquitin Ligase Complex can mediate proteasomal degradation of ORF6, leading to inhibition of viral replication. Moreover, the CUL4B activator etoposide alleviates disease development in a mouse infection model, suggesting that this agent or its derivatives may be used to treat infections caused by SARS-CoV-2. We believe that these results will be extremely useful for the scientific and clinic communities in their search for cues and preventive measures to combat the COVID-19 pandemic.
严重急性呼吸综合征冠状病毒 2(SARS-CoV-2)的辅助蛋白 ORF6 是一种关键的干扰素(IFN)拮抗剂,它强烈抑制初级 IFN 的产生和 IFN 刺激基因的表达。然而,宿主细胞对 ORF6 的反应如何在很大程度上仍是未知的。我们通过下拉法研究 ORF6 结合蛋白的结果表明,E3 连接酶成分,如 Cullin 4B(CUL4B)、DDB1 和 RBX1,是潜在的 ORF6 相互作用蛋白。进一步的研究发现,底物识别受体 PRPF19 与 CUL4B、DDB1 和 RBX1 相互作用形成一个基于 CRL4B 的 E3 连接酶,该酶催化 ORF6 的泛素化和随后的降解。PRPF19 的过表达促进 ORF6 的降解,释放 ORF6 介导的 IFN 抑制,从而抑制 SARS-CoV-2 的复制。此外,我们发现,Etoposide 通过对 CUL4B 的 neddylation 激活来减轻 SARS-CoV-2 小鼠感染模型中的肺损伤。因此,针对 ORF6 的降解可能是对抗 SARS-CoV-2 感染的有效治疗策略。
重要性
泛素-蛋白酶体途径作为调节许多基本细胞过程的重要调节剂的细胞生物学功能已得到广泛认可。泛素-蛋白酶体途径在病毒发病机制中的关键作用已变得越来越明显。它是宿主细胞用来抵御病毒感染的一种强大工具。一些细胞蛋白可以作为限制因子,通过泛素依赖性降解来限制病毒感染。在这项研究中,我们鉴定了 CUL4B-DDB1-PRPF19 E3 泛素连接酶复合物可以介导 ORF6 的蛋白酶体降解,从而抑制病毒复制。此外,CUL4B 激活剂依托泊苷在小鼠感染模型中缓解疾病发展,表明该药物或其衍生物可用于治疗由 SARS-CoV-2 引起的感染。我们相信,这些结果对于科学界和临床界寻找对抗 COVID-19 大流行的线索和预防措施将非常有用。