JVI Accepts, published online ahead of print on 23 April 2008

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J. Virol. doi:10.1128/JVI.00455-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for HSV-1 prereplicative site formation

Christine M. Livingston, Neal A. DeLuca, Dianna E. Wilkinson, and Sandra K. Weller^*

Department of Molecular, Microbial and Structural Biology and The Molecular Biology and Biochemistry Graduate Program, The University of Connecticut Health Center, Farmington CT; Department of Molecular Genetics and Biochemistry, University of Pittsburgh, Pittsburgh PA; Division of Virology, National Institute for Biological Standards and Control, Hertsfordshire, U.K.

^* To whom correspondence should be addressed. Email: weller{at}nso2.uchc.edu.

Herpes simplex virus type 1 (HSV-1) DNA replication occurs in replication compartments that form in the nucleus by an ordered process involving a series of protein scaffold intermediates. Following entry of viral genomes into the nucleus, nucleoprotein complexes containing ICP4 can be detected at a position adjacent to ND10-like bodies. ND10 are then disrupted by the viral E3 ubiquitin ligase ICP0. We have previously reported that after the dissociation of ND10-like bodies, ICP8 could be observed in a diffuse staining pattern; however, using more sensitive staining methods, we now report that in addition to diffuse staining, ICP8 can be detected in tiny foci adjacent to ICP4 foci. ICP8 microfoci contain UL9 and components of the helicase/primase complex. HSV infection also results in the reorganization of the heat shock cognate protein 70 (Hsc70) and the 20S proteasome into virus induced chaperone enriched (VICE) domains. In this report we show that VICE domains are distinct but adjacent to the ICP4 nucleoprotein complexes and the ICP8 microfoci. In cells infected with an ICP4 mutant virus encoding a mutant protein that cannot oligomerize on DNA, ICP8 microfoci are not detected; however, VICE domains could still be formed. These results suggest that oligomerization of ICP4 on viral DNA may be essential for the formation of ICP8 microfoci but not for the reorganization of host cell chaperones into VICE domains.

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