Autor: |
Haskell KM; Department of Cancer Research, Merck Research Laboratories, West Point, Pennsylvania 19486., Vuocolo GA, Defeo-Jones D, Jones RE, Ivey-Hoyle M |
Jazyk: |
angličtina |
Zdroj: |
The Journal of general virology [J Gen Virol] 1993 Jan; Vol. 74 ( Pt 1), pp. 115-9. |
DOI: |
10.1099/0022-1317-74-1-115 |
Abstrakt: |
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. |
Databáze: |
MEDLINE |
Externí odkaz: |
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