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Journal of Virology, June 2002, p. 5598-5604, Vol. 76, No. 11
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.11.5598-5604.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Acidic Activation Domain of the Baculovirus Transactivator IE1 Contains a Virus-Specific Domain Essential for DNA Replication{dagger}

Joseph A. Pathakamuri1 and David A. Theilmann1,2*

Pacific Agri-Food Research Centre, Agriculture and Agri-Food Canada, Summerland, British Columbia, Canada V0H 1Z0,2 Department of Plant Science, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z41

Received 18 December 2001/ Accepted 1 March 2002

IE1 is a potent transcriptional transactivator of the baculovirus Orgyia pseudotsugata multiple nucleopolyhedrovirus (OpMNPV) and has been shown to be essential for viral DNA replication. IE1 contains an acidic activation domain (AAD) at the N terminus that is essential for transcriptional transactivation, but its role in viral DNA replication is unknown. In this study the role of the IE1 AAD in DNA replication is investigated. We have determined that deletion of the AAD eliminates the ability of IE1 to support DNA replication, showing that the AAD is essential for DNA replication as well as transcriptional transactivation. Replacement of the AAD with the archetype domain from herpesvirus VP16 and the evolutionarily related domain from Autographa californica MNPV (AcMNPV) IE1 produces chimeric proteins that are potent transactivators. Surprisingly, however, these chimeric proteins were unable to support DNA replication, indicating that there is a host- or virus-specific replication subdomain in the AAD that was not functionally replaced by the VP16 or AcMNPV AAD. Using N- and C-terminal deletion mutants, the region of the AAD that was essential for DNA replication was mapped to amino acids 1 to 65. AAD deletion mutants also showed that an IE1 that is functional for transcriptional transactivation is not required for viral DNA replication. The IE1 AAD therefore contains an essential replication domain that is separable from the transcriptional activation domains. Our results suggest that IE1 specifically interacts with a component of the viral replication complex, supporting the view that it acts as a nucleating factor by binding to the viral replication origins.

* Corresponding author. Mailing address: Pacific Agri-Food Research Centre Agriculture and Agri-Food Canada, 4200 Highway 97, Summerland, BC V0H 1Z0, Canada. Phone: (250) 494-6395. Fax: (250) 494-0755. E-mail: TheilmannD{at}em.agr.ca.

{dagger} This paper is contribution no. 2150 from the Pacific Agri-Food Research Centre.

Journal of Virology, June 2002, p. 5598-5604, Vol. 76, No. 11
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.11.5598-5604.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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