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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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