Journal of General Virology, Vol 79, 371-374, Copyright © 1998 by Society for General Microbiology

ARTICLES

The identification of a conserved binding motif within human papillomavirus type 16 E6 binding peptides, E6AP and E6BP

RC Elston, S Napthine and J Doorbar
Division of Virology, National Institute for Medical Research, London, UK. relston@nimr.mrc.ac.uk

A 16-mer peptide library was screened using the yeast two-hybrid system to identify peptides which specifically interact with the human papillomavirus type 16 (HPV-16) E6 protein. Four different peptides were identified, three of which contained an E-L-L/V-G motif. A fifth E6 binding peptide, derived from the putative tumour suppressor protein tuberin, was identified during a two-hybrid screen of a HeLa cDNA expression library. This peptide contained a D-I-L-G motif. Homology to the peptides was found within the E6 binding proteins E6-AP and E6-BP. A synthetic peptide containing the ELLG motif blocked the interaction of E6 with both E6-AP and E6-BP. The data suggest that E6 interacts through a structurally similar binding domain present within a number of cellular proteins.

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