Fontaine-Rodriguez Errin C, Taylor Travis J, Olesky Melanie, Knipe David M
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
Virology. 2004 Dec 20;330(2):487-92. doi: 10.1016/j.virol.2004.10.002.
The herpes simplex virus (HSV) immediate early ICP27 protein plays an essential role in stimulating viral early and late gene expression. ICP27 appears to be multifunctional in that it has been reported to stimulate viral late gene transcription, polyadenylation site usage, and RNA export. We report here on proteomic studies involving immunoprecipitation of ICP27 and mass spectrometric identification of co-precipitated proteins. These studies show an association of ICP27 with the cellular translation initiation factors poly A binding protein (PABP), eukaryotic initiation factor 3 (eIF3), and eukaryotic initiation factor 4G (eIF4G) in infected cells. Immunoprecipitation-western blot studies confirmed these associations. Finally, purified MBP-tagged ICP27 (MBP-27) can interact with eIF3 subunits p47 and p116 in vitro. These results suggest that ICP27 may also play a role in stimulating translation of certain viral and host mRNAs and/or in inhibiting host mRNA translation.
单纯疱疹病毒（HSV）即刻早期ICP27蛋白在刺激病毒早期和晚期基因表达中起关键作用。ICP27似乎具有多种功能，因为据报道它能刺激病毒晚期基因转录、多聚腺苷酸化位点的使用以及RNA输出。我们在此报告蛋白质组学研究，该研究涉及ICP27的免疫沉淀和共沉淀蛋白的质谱鉴定。这些研究表明，在受感染细胞中，ICP27与细胞翻译起始因子多聚腺苷酸结合蛋白（PABP）、真核起始因子3（eIF3）和真核起始因子4G（eIF4G）存在关联。免疫沉淀-蛋白质印迹研究证实了这些关联。最后，纯化的MBP标记的ICP27（MBP-27）在体外可与eIF3亚基p47和p116相互作用。这些结果表明，ICP27可能在刺激某些病毒和宿主mRNA的翻译和/或抑制宿主mRNA翻译中也发挥作用。
