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J Gen Virol 71 (1990), 1817-1821; DOI 10.1099/0022-1317-71-8-1817
© 1990 Society for General Microbiology

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Papillomavirus Trans-activator Protein E2 Activates Expression from the Promoter for the Ribonucleotide Reductase Large Subunit from Herpes Simplex Virus Type 2

James P. Wymer1 and Laure Aurelian1,2,

1 Virology/Immunology Laboratories, Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore, Maryland 21201
and2 Divisions of Biophysics and Comparative Medicine, The Johns Hopkins Medical Institutions, Baltimore, Maryland 21205, U.S.A.

Activation of the herpes simplex virus type 2 (HSV-2) large subunit of the ribonucleotide reductase (ICP10) gene by papillomavirus DNA encoding the E2 or E7 proteins was studied directly by immunofluorescence or by chloramphenicol acetyltransferase (CAT) analysis with hybrid ICP10 or IE175 and 38K promoter constructions. Cotransfection with bovine papillomavirus type 1 or human papillomavirus type 16(HPV-16) E2 DNA enhanced CAT expression from constructions in which CAT is regulated by the ICP10 but not by other HSV promoters. Expression was not enhanced by cotransfection with HPV-16 E7 DNA. Sequence analysis of the ICP10 promoter identified a consensus E2-binding motif. Activation was significantly reduced by site-directed mutagenesis of the consensus motif.

Received 12 January 1990; accepted 27 March 1990.





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