Hammarskjöld M L, Simurda M C
Department of Microbiology, State University of New York, Buffalo 14214.
J Virol. 1992 Nov;66(11):6496-501. doi: 10.1128/JVI.66.11.6496-6501.1992.
The Epstein-Barr virus latent membrane protein (LMP) is an integral membrane protein that is expressed in cells latently infected with the virus. LMP is believed to play an important role in Epstein-Barr virus transformation and has been shown to induce expression of several cellular proteins. We performed a series of experiments that demonstrated that LMP is an efficient transactivator of expression from the human immunodeficiency virus type 1 long terminal repeat (HIV-1 LTR). Mutation or deletion of the NF-kappa B elements in the LTR abolished the transactivation, indicating that the LMP effect on HIV expression was due to induction of NF-kappa B activity. Experiments in which the HIV-1 Tat protein was coexpressed in cells together with LMP showed that Tat was able to potentiate the transactivation. Surprisingly, a synergistic effect of the two proteins was observed even in the absence of the recognized target region for Tat (TAR) in the HIV-1 LTR.
爱泼斯坦-巴尔病毒潜伏膜蛋白(LMP)是一种整合膜蛋白,在被该病毒潜伏感染的细胞中表达。LMP被认为在爱泼斯坦-巴尔病毒转化过程中起重要作用,并且已显示能诱导多种细胞蛋白的表达。我们进行了一系列实验,证明LMP是人类免疫缺陷病毒1型长末端重复序列(HIV-1 LTR)表达的有效反式激活因子。LTR中NF-κB元件的突变或缺失消除了反式激活作用,表明LMP对HIV表达的影响是由于诱导了NF-κB活性。在细胞中同时共表达HIV-1 Tat蛋白和LMP的实验表明,Tat能够增强反式激活作用。令人惊讶的是,即使在HIV-1 LTR中不存在公认的Tat靶区域(TAR)的情况下,也观察到了这两种蛋白的协同效应。