THE IDENTIFICATION OF A CONSERVED BINDING MOTIF WITHIN HUMAN-PAPILLOMAVIRUS TYPE-16 E6 BINDING PEPTIDES, E6AP AND E6BP

A 16-mer peptide library was screened using the yeast two-hybrid syste m to identify peptides which specifically interact with the human papi llomavirus type 16 (HPV-16) E6 protein. Four different peptides were i dentified, three of which contained an EL-L/V-G motif. A fifth E6 bind ing peptide, derived from the putative tumour suppressor protein tuber in, was identified during a two-hybrid screen of a HeLa cDNA expressio n library. This peptide contained a D-I-L-G motif. Homology to the pep tides was found within the E6 binding proteins E6AP and EG-BP. A synth etic peptide containing the ELLG motif blocked the interaction of E6 w ith both EG-AP and E6-BP. The data suggest that E6 interacts through a structurally similar binding domain present within a number of cellul ar proteins.