Brokaw J L, Yee C L, Münger K
Laboratory of Tumor Virus Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
Virology. 1994 Dec;205(2):603-7. doi: 10.1006/viro.1994.1688.
The human papillomavirus type 16 (HPV-16) E7 oncoprotein shares structural and functional similarity with the adenovirus (Ad) E1A protein and the SV40 large tumor antigen (TAg). Like these other DNA tumor virus oncoproteins, HPV-16 E7 interacts with the "pocket proteins," a family of host cellular proteins that include the retinoblastoma tumor suppressor protein and can cooperate with the ras oncogene to transform primary rodent cells. Mutational analyses have indicated that amino acid sequences outside of the pRB binding region are also important for the cellular transformation property of HPV-16 E7. These sequences include an amino terminal domain of the E7 protein that is similar to a portion of conserved region 1 of Ad E1A. In this study it is shown that the homologous amino acid sequences in Ad E1A and SV40 TAg are functionally interchangeable with the amino terminal HPV-16 E7 domain in transformation assays. Deletion analysis across the amino terminus of HPV-16 E7 indicated that the overall integrity of the entire CR1 homology domain is important for the biological activity of the HPV E7 oncoprotein.
人乳头瘤病毒16型（HPV - 16）E7癌蛋白与腺病毒（Ad）E1A蛋白以及猴空泡病毒40大T抗原（TAg）在结构和功能上具有相似性。与这些其他DNA肿瘤病毒癌蛋白一样，HPV - 16 E7与“口袋蛋白”相互作用，“口袋蛋白”是一类宿主细胞蛋白，包括视网膜母细胞瘤肿瘤抑制蛋白，并且可以与ras癌基因协同作用来转化原代啮齿动物细胞。突变分析表明，pRB结合区域之外的氨基酸序列对于HPV - 16 E7的细胞转化特性也很重要。这些序列包括E7蛋白的氨基末端结构域，该结构域与Ad E1A保守区域1的一部分相似。在本研究中表明，在转化试验中，Ad E1A和SV40 TAg中的同源氨基酸序列与HPV - 16 E7氨基末端结构域在功能上是可互换的。对HPV - 16 E7氨基末端进行的缺失分析表明，整个CR1同源结构域的整体完整性对于HPV E7癌蛋白的生物学活性很重要。
