Papillomavirus E7 protein binding to the retinoblastoma protein is not required for viral induction of warts

Defeo-Jones, Deborah; Vuocolo, G A; Haskell, Kathleen; Hanobik, Michelle G.; Kiefer, David M.; McAvoy, Elizabeth; Ivey-Hoyle, Mona; Brandsma, Janet L.; Oliff, Allen; Jones, Raymond E.

doi:10.1128/jvi.67.2.716-725.1993

Cited by 63 publications

(27 citation statements)

References 75 publications

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“…able to bind IGFBP-3 and trigger its degradation. This finding suggests that the interaction of E7 with the retinoblastoma family of proteins is not required for inactivation of IGFBP-3 and strengthens the notion that several distinct regulatory pathways must be subverted by E7 in order to transform mammalian cells, in keeping with the results from numerous genetic (7,8,17,20,25,41,84) and biochemical (4,5,14,19,24,28,42,54,65,79,89,93,94) studies (for a recent review, see reference 91).…”

Section: Discussionsupporting

confidence: 63%

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Human Papillomavirus Type 16 E7 Oncoprotein Binds and Inactivates Growth-Inhibitory Insulin-Like Growth Factor Binding Protein 3

et al. 2000

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The E7 protein encoded by human papillomavirus type 16 is one of the few viral genes that can immortalize primary human cells and thereby override cellular senescence. While it is generally assumed that this property of E7 depends on its interaction with regulators of the cell cycle, we show here that E7 targets insulin-like growth factor binding protein 3 (IGFBP-3), the product of a p53-inducible gene that is overexpressed in senescent cells. IGFBP-3 can suppress cell proliferation and induce apoptosis; we show here that IGFBP-3mediated apoptosis is inhibited by E7, which binds to IGFBP-3 and triggers its proteolytic cleavage. Two transformation-deficient mutants of E7 failed to inactivate IGFBP-3, suggesting that inactivation of IGFBP-3 may contribute to cell transformation.

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Section: Discussionsupporting

confidence: 63%

“…Cell lysates were prepared and subjected to immunoprecipitation with antibodies to E7 and IGFBP-3 and control antibodies, as indicated. Precipitated proteins were detected by Western blotting.VOL 20,. 2000 HPV-16 E7 BINDS AND INACTIVATES IGF-BINDING PROTEIN also drastically reduced in the supernatants of E7-expressing cells.…”

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confidence: 99%

Human Papillomavirus Type 16 E7 Oncoprotein Binds and Inactivates Growth-Inhibitory Insulin-Like Growth Factor Binding Protein 3

et al. 2000

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“…Analogous data were obtained using the cottontail rabbit papillomavirus (CRPV) model. In these studies mutants of CRPV E7, which were not able to bind Rbl , were still able to induce wart formation in rabbits (29). The data obtained suggest that the interaction of Rbl is not important in the early state of the infection cycle.…”

Section: E7/rb 1 Interaction and Cellular Transformationmentioning

confidence: 80%

Human Papillomavirus E6 and E7: Proteins which deregulate the cell cycle

1995

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Numerous clinical, epidemiological and molecular findings link some types of Human Papillomaviruses (HPV) with cancer of the genital tract. They share a common pathway of transformation with a number of DNA tumour viruses, such as Adenovirus and SV40. Although all these viruses are termed 'DNA tumour viruses' and have similar in vitro transforming activities, Human Papillomavirus is the only one so far clearly involved in human cancer. Extensive studies on HPV E6 and E7 proteins have demonstrated their involvement in malignant transformation. E6 and E7 bind the products of tumour suppressor genes, p53 and Rb1, respectively, modifying or inactivating their normal functions. The Rb1 and p53 genes are deleted or mutated in several cancers and both proteins regulate the transcription of genes involved in cell cycle progression control. The E6/p53 and E7/Rb1 interactions result in a deregulation of the cell cycle with loss of control of crucial cellular events, such as DNA replication, DNA repair and apoptosis.

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“…Whereas binding of the Rb protein family by E7 is mediated by conserved domain 2 of the viral protein, it was shown that functional inactivation of pRb also requires sequences in the very N-terminal and the C-terminal part of E7, in addition to the pRbbinding interface (17,25). The C-terminal half of the E7 protein is essential for immortalization and transformation of human cells (26,27). Whereas the mechanisms by which the C-terminal domain of E7 contributes to cell transformation are not entirely clear, numerous cellular regulatory proteins have been identified, which are bound by E7 via its C-terminal part.…”

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confidence: 99%

Induction of apoptosis in cervical carcinoma cells by peptide aptamers that bind to the HPV‐16 E7 oncoprotein

2001

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Human papillomaviruses (HPV) of the high-risk type are causally involved in human tumors, in particular cervical carcinoma. Expression of the viral oncogenes E6 and E7 is maintained in HPV-positive tumors, and it was shown that E6 and E7 of HPV-16 can immortalize human keratinocytes, the natural host cells of the virus. Expression of the viral genes is also required for maintenance of the transformed phenotype. The oncogenic activity of the E6 and E7 oncoproteins is mediated by their physical and functional interaction with cellular regulatory proteins. To knock out the function of the E7 protein in living cells, we have developed peptide aptamers with high specific binding activity for the E7 protein of HPV-16. We show here that E7-binding peptide aptamers induce programmed cell death (apoptosis) in E7-expressing cells, whereas E7-negative cells are not affected. Furthermore, E7-binding peptide aptamers induce apoptosis in HPV-16-positive tumor cells derived from cervical carcinoma. The data suggest that E7-binding peptide aptamers may be useful tools to specifically eliminate HPV-positive tumors.

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Papillomavirus E7 protein binding to the retinoblastoma protein is not required for viral induction of warts

Cited by 63 publications

References 75 publications

Human Papillomavirus Type 16 E7 Oncoprotein Binds and Inactivates Growth-Inhibitory Insulin-Like Growth Factor Binding Protein 3

Human Papillomavirus Type 16 E7 Oncoprotein Binds and Inactivates Growth-Inhibitory Insulin-Like Growth Factor Binding Protein 3

Human Papillomavirus E6 and E7: Proteins which deregulate the cell cycle

Induction of apoptosis in cervical carcinoma cells by peptide aptamers that bind to the HPV‐16 E7 oncoprotein

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