Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
Mol Cell Proteomics. 2010 Sep;9(9):1920-36. doi: 10.1074/mcp.M900345-MCP200. Epub 2010 May 13.
Virus-host interactions involve complex interplay between viral and host factors, rendering them an ideal target for proteomic analysis. Here we detail a high throughput quantitative proteomics analysis of Vero cells infected with the coronavirus infectious bronchitis virus (IBV), a positive strand RNA virus that replicates in the cytoplasm. Stable isotope labeling with amino acids in cell culture (SILAC) was used in conjunction with LC-MS/MS to identify and quantify 1830 cellular and two viral proteins from IBV-infected cells. Fractionation of cells into cytoplasmic, nuclear, and nucleolar extracts was used to reduce sample complexity and provide information on the trafficking of proteins between the different compartments. Each fraction showed a proportion of proteins exhibiting >or=2-fold changes in abundance. Ingenuity Pathway Analysis revealed that proteins that changed in response to infection could be grouped into different functional categories. These included proteins regulated by NF-kappaB- and AP-1-dependent pathways and proteins involved in the cytoskeleton and molecular motors. A luciferase-based reporter gene assay was used to validate the up-regulation of AP-1- and NF-kappaB-dependent transcription in IBV-infected cells and confirmed using immunofluorescence. Immunofluorescence was used to validate changes in the subcellular localization of vimentin and myosin VI in IBV-infected cells. The proteomics analysis also confirmed the presence of the viral nucleocapsid protein as localizing in the cytoplasm, nucleus, and nucleolus and the viral membrane protein in the cytoplasmic fraction. This research is the first application of SILAC to study total host cell proteome changes in response to positive sense RNA virus infection and illustrates the versatility of this technique as applied to infectious disease research.
病毒-宿主相互作用涉及病毒和宿主因素之间的复杂相互作用,使其成为蛋白质组学分析的理想目标。在这里,我们详细介绍了冠状病毒传染性支气管炎病毒(IBV)感染的vero 细胞的高通量定量蛋白质组学分析,IBV 是一种在细胞质中复制的正链 RNA 病毒。稳定同位素标记与细胞培养中的氨基酸(SILAC)与 LC-MS/MS 结合使用,从 IBV 感染的细胞中鉴定和定量了 1830 种细胞和两种病毒蛋白。将细胞分为细胞质、核和核仁提取物,以降低样品复杂性并提供蛋白质在不同隔室之间运输的信息。每个分数都显示出比例>或= 2 倍变化的蛋白质。Ingenuity Pathway Analysis 显示,对感染有反应的蛋白质可以分为不同的功能类别。这些包括受 NF-kappaB-和 AP-1 依赖性途径调节的蛋白质以及参与细胞骨架和分子马达的蛋白质。基于荧光素酶的报告基因测定用于验证 IBV 感染细胞中 AP-1 和 NF-kappaB 依赖性转录的上调,并通过免疫荧光进行验证。免疫荧光用于验证 IBV 感染细胞中波形蛋白和肌球蛋白 VI 的亚细胞定位变化。蛋白质组学分析还证实了病毒核衣壳蛋白存在于细胞质、细胞核和核仁中,以及病毒膜蛋白存在于细胞质部分。这项研究是首次应用 SILAC 研究阳性 sense RNA 病毒感染后总宿主细胞蛋白质组的变化,并说明了该技术在传染病研究中的多功能性。