爱泼斯坦-巴尔病毒（EBV）复制起点（oriP）与EBNA-1及细胞抗EBNA-1蛋白的相互作用。

Interaction of Epstein-Barr viral (EBV) origin of replication (oriP) with EBNA-1 and cellular anti-EBNA-1 proteins.

作者信息

Wen L T, Lai P K, Bradley G, Tanaka A, Nonoyama M

机构信息

Laboratory of Virology, Tampa Bay Research Institute, St. Petersburg, Florida 33716.

出版信息

Virology. 1990 Sep;178(1):293-6. doi: 10.1016/0042-6822(90)90407-i.

DOI:10.1016/0042-6822(90)90407-i

PMID:2167556

Abstract

We have previously shown that 12-O-tetradecanoylphorbol-13-acetate (TPA) which activates expression of the latent genome of the Epstein-Barr virus (EBV) in Burkitt lymphoma cells induces the synthesis of two cellular anti-EBNA-1 competitor proteins, anti-EBNA-1.1 and anti-EBNA-1.2. Both anti-EBNA-1 proteins can uncouple the specific binding of the EBNA-1 to the region required for EBV plasmid maintenance (oriP). Here, we show by DNase I footprinting that the binding sites on oriP for the EBNA-1 and the anti-EBNA-1 proteins were indistinguishable. The proteins bound to the 30-bp tandem repeats of the oriP. Glycerol-gradient centrifugation and gel retardation assay revealed that a 60-kDa protein formed the anti-EBNA-1.1-DNA complex and a 40-kDa protein formed the anti-EBNA-1.2-DNA complex.

摘要

我们之前已经表明，12-O-十四烷酰佛波醇-13-乙酸酯（TPA）可激活伯基特淋巴瘤细胞中爱泼斯坦-巴尔病毒（EBV）潜伏基因组的表达，它能诱导两种细胞抗EBNA-1竞争蛋白，即抗EBNA-1.1和抗EBNA-1.2的合成。这两种抗EBNA-1蛋白均可使EBNA-1与EBV质粒维持所需区域（oriP）的特异性结合解偶联。在此，我们通过DNA酶I足迹法表明，oriP上EBNA-1和抗EBNA-1蛋白的结合位点无法区分。这些蛋白与oriP的30 bp串联重复序列结合。甘油梯度离心和凝胶阻滞分析显示，一种60 kDa的蛋白形成抗EBNA-1.1-DNA复合物，一种40 kDa的蛋白形成抗EBNA-1.2-DNA复合物。