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J Gen Virol 77 (1996), 1805-1809; DOI 10.1099/0022-1317-77-8-1805
© 1996 Society for General Microbiology

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Characterization of the helicase and ATPase activity of human papillomavirus type 6b E1 protein

Owen Jenkins1, David Earnshaw2, Gillian Sarginson1, Alfred Del Vecchio3, Jane Tsai3, Howard Kallender1, Bernard Amegadzie4 and Michael Browne2

1 SmithKline Beecham Pharmaceuticals, Department of Biotechnology, Yew Tree Bottom Road, Epsom, Surrey KT18 5XQ, UK
2 New Frontiers Science Park North, Third Avenue, Harlow, Essex CM19 5AW, UK
3 Department of Molecular Virology & Host Defence
4 Department of Gene Expression Sciences, Upper Merion, 709 Swedeland Road, King of Prussia, PA 194 06, USA

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

Received 1 March 1996; accepted 12 March 1996.


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