CHARACTERIZATION OF THE HELICASE AND ATPASE ACTIVITY OF HUMAN PAPILLOMAVIRUS TYPE 6B E1 PROTEIN

Human papillomavirus type 6b (HPV-6b) is one of the most common causes of human genital warts, an important sexually transmitted disease. Di scovery of antiviral therapies for this condition has been hampered by the inability to propagate the virus using standard tissue culture te chniques and through difficulties in expressing sufficient recombinant viral proteins in vitro. Replication of papillomavirus DNA requires t wo viral proteins, E1 and E2. In an effort to establish assays to disc over compounds active against this virus, we have coexpressed HPV-6b E 1 and E2 proteins in insect cells. We demonstrate that the two protein s form a heteromeric complex which can be purified by sequence-specifi c DNA affinity chromatography. We also demonstrate that the complex ha s both E1-associated ATPase and ATP-dependent DNA helicase activity an d report further characterization of these functions.