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Journal of Virology, March 2001, p. 2353-2367, Vol. 75, No. 5
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.5.2353-2367.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Interactions of Herpes Simplex Virus Type 1 with ND10 and Recruitment of PML to Replication Compartments

Jennifer Burkham,1 Donald M. Coen,2 Charles B. C. Hwang,3 and Sandra K. Weller1,*

Department of Microbiology, University of Connecticut Health Center, Farmington, Connecticut 060301; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 021152; and Upstate Medical University, State University of New York, Syracuse, New York 132103

Received 6 June 2000/Accepted 6 December 2000

Many of the events required for productive herpes simplex virus type 1 (HSV-1) infection occur within globular nuclear domains called replication compartments, whose formation appears to depend on interactions with cellular nuclear domains 10 (ND10). We have previously demonstrated that the formation of HSV-1 replication compartments involves progression through several stages, including the disruption of intact ND10 (stage I to stage II) and the formation of PML-associated prereplicative sites (stage III) and replication compartments (stage IV) (J. Burkham, D. M. Coen, and S. K. Weller, J. Virol. 72:10100-10107, 1998). In this paper, we show that some, but not all, PML isoforms are recruited to stage III foci and replication compartments. Genetic experiments showed that the recruitment of PML isoforms to stage III prereplicative sites and replication compartments requires the localization of the HSV-1 polymerase protein (UL30) to these foci but does not require polymerase catalytic activity. We also examined the stages of viral infection under conditions affecting ND10 integrity. Treatment with factors that increase the stability of ND10, arsenic trioxide and the proteasome inhibitor MG132, inhibited viral disruption of ND10, formation of replication compartments, and production of progeny virus. These results strengthen the previously described correlation between ND10 disruption and productive viral infection.

* Corresponding author. Mailing address: Department of Microbiology, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06030. Phone: (860) 679-2310. Fax: (860) 679-1239. E-mail: Weller{at}NSO2.uchc.edu.

Journal of Virology, March 2001, p. 2353-2367, Vol. 75, No. 5
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.5.2353-2367.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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