Division of Molecular and Cell Biology, School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Mol Cell Proteomics. 2010 Sep;9(9):1829-48. doi: 10.1074/mcp.M110.001651. Epub 2010 Jun 8.
In this study, we used imaging and proteomics to identify the presence of virus-associated cellular proteins that may play a role in respiratory syncytial virus (RSV) maturation. Fluorescence microscopy of virus-infected cells revealed the presence of virus-induced cytoplasmic inclusion bodies and mature virus particles, the latter appearing as virus filaments. In situ electron tomography suggested that the virus filaments were complex structures that were able to package multiple copies of the virus genome. The virus particles were purified, and the protein content was analyzed by one-dimensional nano-LC MS/MS. In addition to all the major virus structural proteins, 25 cellular proteins were also detected, including proteins associated with the cortical actin network, energy pathways, and heat shock proteins (HSP70, HSC70, and HSP90). Representative actin-associated proteins, HSC70, and HSP90 were selected for further biological validation. The presence of beta-actin, filamin-1, cofilin-1, HSC70, and HSP90 in the virus preparation was confirmed by immunoblotting using relevant antibodies. Immunofluorescence microscopy of infected cells stained with antibodies against relevant virus and cellular proteins confirmed the presence of these cellular proteins in the virus filaments and inclusion bodies. The relevance of HSP90 to virus infection was examined using the specific inhibitors 17-N-Allylamino-17-demethoxygeldanamycin. Although virus protein expression was largely unaffected by these drugs, we noted that the formation of virus particles was inhibited, and virus transmission was impaired, suggesting an important role for HSP90 in virus maturation. This study highlights the utility of proteomics in facilitating both our understanding of the role that cellular proteins play during RSV maturation and, by extrapolation, the identification of new potential targets for antiviral therapy.
在这项研究中,我们使用成像和蛋白质组学来鉴定可能在呼吸道合胞病毒 (RSV) 成熟过程中发挥作用的病毒相关细胞蛋白。病毒感染细胞的荧光显微镜显示存在病毒诱导的细胞质包涵体和成熟的病毒颗粒,后者表现为病毒丝。原位电子断层扫描表明,病毒丝是能够包装多个病毒基因组拷贝的复杂结构。病毒颗粒被纯化,通过一维纳升 LC-MS/MS 分析蛋白质含量。除了所有主要的病毒结构蛋白外,还检测到 25 种细胞蛋白,包括与皮质肌动蛋白网络、能量途径和热休克蛋白 (HSP70、HSC70 和 HSP90) 相关的蛋白。选择代表性的肌动蛋白相关蛋白 HSC70 和 HSP90 进行进一步的生物学验证。使用相关抗体进行免疫印迹,证实了病毒制剂中存在 beta-肌动蛋白、丝联蛋白-1、原肌球蛋白-1、HSC70 和 HSP90。用针对相关病毒和细胞蛋白的抗体对感染细胞进行免疫荧光显微镜染色,证实了这些细胞蛋白存在于病毒丝和包涵体中。使用特异性抑制剂 17-N-烯丙基-17-去甲氧基格尔德霉素 (17-N-Allylamino-17-demethoxygeldanamycin) 研究 HSP90 与病毒感染的相关性。尽管这些药物对病毒蛋白表达的影响不大,但我们注意到病毒颗粒的形成受到抑制,病毒传播受损,表明 HSP90 在病毒成熟过程中起着重要作用。这项研究强调了蛋白质组学在促进我们对细胞蛋白在 RSV 成熟过程中所起作用的理解以及推断新的抗病毒治疗潜在靶标的应用。