Complex-Formation of Human Papillomavirus-E7 Proteins with the Retinoblastoma Tumor Suppressor Gene-Product

Munger, K., Werness, B. A., Dyson, N., Phelps, W. C., Harlow, E., Howley, P. M. (December 1989) Complex-Formation of Human Papillomavirus-E7 Proteins with the Retinoblastoma Tumor Suppressor Gene-Product. Embo Journal, 8 (13). pp. 4099-4105. ISSN 0261-4189

URL: http://www.ncbi.nlm.nih.gov/pubmed/2556261

Abstract

The E7 proteins encoded by the human papillomaviruses (HPVs) associated with anogenital lesions share significant amino acid sequence homology. The E7 proteins of these different HPVs were assessed for their ability to form complexes with the retinoblastoma tumor suppressor gene product (p105-RB). Similar to the E7 protein of HPV-16, the E7 proteins of HPV-18, HBV-6b and HPV-11 were found to associate with p105-RB in vitro. The E7 proteins of HPV types associated with a high risk of malignant progression (HPV-16 and HPV-18) formed complexes with p105-RB with equal affinities. The E7 proteins encoded by HPV types 6b and 11, which are associated with clinical lesions with a lower risk for progression, bound to p105-RB with lower affinities. The E7 protein of the bovine papillomavirus type 1 (BPV-1), which does not share structural similarity in the amino terminal region with the HPV E7 proteins, was unable to form a detectable complex with p105-RB. The amino acid sequences of the HPV-16 E7 protein involved in complex formation with p105-RB in vitro have been mapped. Only a portion of the sequences that are conserved between the HPV E7 proteins and AdE1A were necessary for association with p105-RB. Furthermore, the HPV-16 E7-p105-RB complex was detected in an HPV-16-transformed human keratinocyte cell line.

Item Type: Paper
Subjects: organism description > animal > mammal > primates > hominids > human
organism description > virus > papillomavirus
diseases & disorders > cancer > cancer types > retinoblastoma
CSHL Authors:
Communities: CSHL labs
Depositing User: Gail Sherman
Date: 20 December 1989
Date Deposited: 23 Jun 2017 20:04
Last Modified: 23 Jun 2017 20:04
PMCID: PMC401588
URI: http://repository.cshl.edu/id/eprint/34888

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