中文摘要：

在宿指胞的信使 rna 翻译的 HSV-1 调停感染的规定是一系统；复杂过程。这机制的细节的调查将在病毒的复制过程便于生物变化的理解；宿指胞。在这研究，一个比较 proteomics 技术平台被 HSV-1 的二尺寸的电气泳动使用感染的正常人的 L-02 房间；控制房间 lysates。观察蛋白质点是分析品质上；由 PDQuest 软件包裹的份量上。很多仔细与细胞的蛋白质合成联系的不同观察蛋白质点被飞行团 spectrometry (MALDI-TOF-MS ) 的帮助矩阵的激光解吸附作用电离时间识别。RPLP1 蛋白质的表示层次，为信使 rna 翻译被要求，；而 RNP H2 的表示水平，它在拼接的信使 rna 上涉及正控制处理， KHSRP 蛋白质，涉及信使 rna 的快速的腐烂，是起来调整的，是下面调整的。所有这些结果建议那个 HSV-1 感染罐头经由涉及拼接的 RNA 的细胞的规章的蛋白质的调整影响细胞的蛋白质合成，翻译；腐烂，当细胞的蛋白质合成被关掉时，导致病毒蛋白合成的优化。尽管对关于细胞的蛋白质控制的详细机制的进一步的调查有需要，我们的研究提供新卓见进指向表明涉及主机的小径的改变的病毒细胞的蛋白质合成。

英文摘要：

HSV-1 infection-mediated regulation of mRNA translation in host cells is a systematic and complicated process. Investigation of the details of this mechanism will facilitate understanding of biological variations in the viral replication process and host cells. In this study, a comparative proteomics technology platform was applied by two-dimension electrophoresis of HSV-1 infected normal human L-02 cell and control cell lysates. The observed protein spots were analyzed qualitatively and quantitatively by the PDQuest software package. A number of the different observed protein spots closely associated with cellular protein synthesis were identified by matrix-assisted laser-desorption ionization-time of flight-mass spectrometry （MALDI-TOF-MS）. The expression levels of the RPLP1 protein, which is required for mRNA translation, and KHSRP protein, which is involved in rapid decay of mRNA, were up-regulated, whereas the expression level of RNP H2, which is involved in positive regulation on the mRNA splicing process, was down-regulated. All of these results suggest that HSV-1 infection can influence cellular protein synthesis via modulation of cellular regulatory proteins involved in RNA splicing, translation and decay, resulting in optimisation of viral protein synthesis when cellular protein synthesis is shut off Although there is need for further investigations regarding the detailed mechanisms of cellular protein control, our studies provide new insight into the targeting of varied virus signaling pathways involved in host cellular protein synthesis.