JVI Accepts, published online ahead of print on 11 April 2007
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J. Virol. doi:10.1128/JVI.00380-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Us3 of Herpes Simplex type 1 Encodes a Promiscuous Protein Kinase That Phosphorylates and Alters Localization of Lamin A/C in Infected Cells

Fan Mou, Tom Forest, and Joel D. Baines*

Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853

* To whom correspondence should be addressed. Email: jdb11{at}cornell.edu.


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Abstract

HSV-1 Us3 encodes a serine/threonine kinase, that, when inactivated, causes capsids to aggregate aberrantly between the inner and outer nuclear membranes (INM and ONM, respectively) within evaginations/extensions of the perinuclear space. In both Hep2 cells and an engineered cell line derived from Hep2 cells expressing lamin A/C fused to eGFP- lamin A/C localized mostly in a reticular pattern with small regions of the INM devoid of eGFP-lamin A/C when either mock infected or infected with wild type HSV-1(F). Cells infected with HSV-1(F) also contained some larger diffuse regions lacking lamin A/C. UL31 and UL34 proteins, markers of potential envelopment sites at the INM and perinuclear virions, localized within the regions devoid of lamin A/C and also in regions containing lamin A/C. Similar to previous observations in Vero cells (Bjerke and Roller, 2006), the UL34 and UL31 proteins localized exclusively in very discrete regions of the nuclear lamina lacking lamin A/C in the absence of US3 kinase activity. To determine how US3 alters lamin A/C distribution, US3 was purified and shown to phosphorylate lamin A/C at multiple sites in vitro, despite the presence of only one putative Us3 kinase consensus site in the lamin A/C sequence. US3 kinase activity was also sufficient to invoke partial solubilization of lamin A/C from permeabilized Hep2 cell nuclei in an ATP -dependent manner. Two dimensional electrophoretic analyses of lamin A/C from infected cells revealed that lamin A/C is phosphorylated in HSV infected cells, and the full spectrum of phosphorylation requires US3 kinase activity. These data suggest that Us3 kinase activity regulates HSV-1 capsid nuclear egress at least in part by phosphorylation of lamin A/C.




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