Santamaría Enrique, Sánchez-Quiles Virginia, Fernández-Irigoyen Joaquín, Corrales Fernando
Proteomics Unit, Biomedical Research Centre, Navarra Health Service Pamplona, Spain.
Front Microbiol. 2012 Mar 20;3:107. doi: 10.3389/fmicb.2012.00107. eCollection 2012.
Like other DNA viruses, herpes simplex virus type 1 (HSV-1) replicates and proliferates in host cells continuously modulating the host molecular environment. Following a sophisticated temporal expression pattern, HSV-1 encodes at least 89 multifunctional proteins that interplay with and modify the host cell proteome. During the last decade, advances in mass spectrometry applications coupled to the development of proteomic separation methods have allowed to partially monitor the impact of HSV-1 infection in human cells. In this review, we discuss the current use of different proteome fractionation strategies to define HSV-1 targets in two major application areas: (i) viral-protein interactomics to decipher viral-protein interactions in host cells and (ii) differential quantitative proteomics to analyze the virally induced changes in the cellular proteome. Moreover, we will also discuss the potential application of high-throughput proteomic approaches to study global proteome dynamics and also post-translational modifications in HSV-1-infected cells that will greatly improve our molecular knowledge of HSV-1 infection.
与其他DNA病毒一样，单纯疱疹病毒1型（HSV-1）在宿主细胞中复制和增殖，不断调节宿主分子环境。遵循复杂的时间表达模式，HSV-1编码至少89种多功能蛋白，这些蛋白与宿主细胞蛋白质组相互作用并对其进行修饰。在过去十年中，质谱应用的进展以及蛋白质组分离方法的发展使得能够部分监测HSV-1感染对人类细胞的影响。在本综述中，我们讨论了当前在两个主要应用领域中使用不同蛋白质组分分离策略来确定HSV-1靶点的情况：（i）病毒-蛋白质相互作用组学，以破译宿主细胞中的病毒-蛋白质相互作用；（ii）差异定量蛋白质组学，以分析病毒诱导的细胞蛋白质组变化。此外，我们还将讨论高通量蛋白质组学方法在研究HSV-1感染细胞中的全局蛋白质组动态以及翻译后修饰方面的潜在应用，这将极大地提高我们对HSV-1感染的分子认识。
