Haskell K M, Vuocolo G A, Defeo-Jones D, Jones R E, Ivey-Hoyle M
Department of Cancer Research, Merck Research Laboratories, West Point, Pennsylvania 19486.
J Gen Virol. 1993 Jan;74 ( Pt 1):115-9. doi: 10.1099/0022-1317-74-1-115.
Binding of the human papillomavirus type 16 (HPV-16) E7 oncoprotein to the retinoblastoma protein (pRb) is thought to be involved in the cellular transformation mediated by HPV-16. Here we show that the E7 protein of the cottontail rabbit papillomavirus (CRPV) binds to the same C-terminal portion of human pRb as HPV-16 E7, and that both the CRPV and HPV-16 E7 proteins bind specifically through similar domains to rabbit pRb. Furthermore, a single amino acid substitution which reduces the binding of HPV-16 E7 to human pRb also abolishes binding of CRPV E7 to both human and rabbit pRb. The biochemical similarities observed between the HPV-16 and CRPV E7 proteins suggest that they are functionally conserved. These results further validate the use of CRPV as an animal model for the study of HPV-mediated disease.
人乳头瘤病毒16型（HPV - 16）E7癌蛋白与视网膜母细胞瘤蛋白（pRb）的结合被认为与HPV - 16介导的细胞转化有关。在此我们表明，棉尾兔乳头瘤病毒（CRPV）的E7蛋白与HPV - 16 E7一样，结合人pRb的相同C末端部分，并且CRPV和HPV - 16 E7蛋白都通过相似结构域与兔pRb特异性结合。此外，一个降低HPV - 16 E7与人pRb结合的单氨基酸取代也消除了CRPV E7与人和兔pRb的结合。在HPV - 16和CRPV E7蛋白之间观察到的生化相似性表明它们在功能上是保守的。这些结果进一步验证了将CRPV用作研究HPV介导疾病的动物模型的用途。
