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J. Virol. doi:10.1128/JVI.00442-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

BAG3, a Host Co-chaperone, Facilitates Varicella Zoster Virus Replication

Department of Microbiology, College of Physicians and Surgeons, Columbia University, 701 W. 168^th St., New York, New York 10032, USA

^* To whom correspondence should be addressed. Email: sjs6{at}columbia.edu.

	Abstract

Varicella zoster virus establishes a lifelong latent infection in the dorsal root ganglia of the host. During latency, a subset of virus encoded regulatory proteins is detected, however, they are excluded from the nucleus. ORF29p, a single-stranded DNA binding protein is one of these latency associated proteins. We searched for cell proteins that interact with ORF29p and identified BAG3. BAG3 and Hsp70/Hsc70 and Hsp90 colocalize with ORF29p in nuclear transcription/replication factories during lytic replication of VZV. Pharmacological intercession of Hsp90 activity with ansamycin antibiotics or depletion of BAG3 by siRNA result in inhibition of virus replication. Replication in BAG3 depleted cell lines is restored by complementation with exogenous BAG3. Alteration of host chaperone activity provides a novel means of regulating virus replication.

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