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Title: Herpes simplex virus 2 VP22 phosphorylation induced by cellular and viral kinases does not influence intracellular localization

Abstract

Phosphorylation of the herpes simplex virus (HSV) VP22 protein is regulated by cellular kinases and the UL13 viral kinase, but the sites at which these enzymes induce phosphorylation of HSV-2 VP22 are not known. Using serine-to-alanine mutants to map phosphorylation sites on HSV-2 VP22 in cells, we made three major observations. First, phosphorylation by a cellular kinase mapped to serines 70, 71, and/or 72 within CKII consensus sites analogous to previously identified phosphorylation sites in HSV-1 VP22. Second, we mapped UL13-mediated phosphorylation of HSV-2 VP22 to serines 28 and 34, describing for the first time UL13-dependent phosphorylation sites on VP22. Third, previously identified VP22-associated cellular kinase sites in HSV-1 VP22 (serines 292 and 294) were not phosphorylated in HSV-2 VP22 (serines 291 and 293). VP22 expressed alone accumulated in the cytoplasm and to a lesser extent in the nucleus. Phosphorylation by endogenous cellular kinase(s) did not alter the localization of VP22. Co-expression of HSV-2 VP22 with active UL13, but not with enzymatically inactive UL13, resulted in nuclear accumulation of VP22 and altered nuclear morphology. Surprisingly, redistribution of VP22 to the nucleus occurred independently of UL13-induced phosphorylation of VP22. The altered nuclear morphology of UL13-expressing cells was not due to apoptosis.more » These results demonstrate that phosphorylation of HSV-2 VP22 at multiple serine residues is induced by UL13 and cellular kinase(s), and that the nuclear/cytoplasmic distribution of VP22 is independent of its phosphorylation status but is controlled indirectly by UL13 kinase activity.« less

Authors:
 [1];  [1];  [1];  [1]
  1. Department of Molecular Microbiology and Immunology, Saint Louis University School of Medicine, St. Louis, MO 63104-1083 (United States)
Publication Date:
OSTI Identifier:
20637181
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 330; Journal Issue: 1; Other Information: DOI: 10.1016/j.virol.2004.08.034; PII: S0042-6822(04)00583-5; Copyright (c) 2004 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ALANINES; APOPTOSIS; CYTOPLASM; HERPES SIMPLEX; MORPHOLOGY; MUTANTS; PHOSPHORYLATION; PHOSPHOTRANSFERASES; SERINE; VIRUSES

Citation Formats

Geiss, Brian J, Cano, Gina L, Tavis, John E, and Morrison, Lynda A. Herpes simplex virus 2 VP22 phosphorylation induced by cellular and viral kinases does not influence intracellular localization. United States: N. p., 2004. Web. doi:10.1016/j.virol.2004.08.034.
Geiss, Brian J, Cano, Gina L, Tavis, John E, & Morrison, Lynda A. Herpes simplex virus 2 VP22 phosphorylation induced by cellular and viral kinases does not influence intracellular localization. United States. https://doi.org/10.1016/j.virol.2004.08.034
Geiss, Brian J, Cano, Gina L, Tavis, John E, and Morrison, Lynda A. 2004. "Herpes simplex virus 2 VP22 phosphorylation induced by cellular and viral kinases does not influence intracellular localization". United States. https://doi.org/10.1016/j.virol.2004.08.034.
@article{osti_20637181,
title = {Herpes simplex virus 2 VP22 phosphorylation induced by cellular and viral kinases does not influence intracellular localization},
author = {Geiss, Brian J and Cano, Gina L and Tavis, John E and Morrison, Lynda A},
abstractNote = {Phosphorylation of the herpes simplex virus (HSV) VP22 protein is regulated by cellular kinases and the UL13 viral kinase, but the sites at which these enzymes induce phosphorylation of HSV-2 VP22 are not known. Using serine-to-alanine mutants to map phosphorylation sites on HSV-2 VP22 in cells, we made three major observations. First, phosphorylation by a cellular kinase mapped to serines 70, 71, and/or 72 within CKII consensus sites analogous to previously identified phosphorylation sites in HSV-1 VP22. Second, we mapped UL13-mediated phosphorylation of HSV-2 VP22 to serines 28 and 34, describing for the first time UL13-dependent phosphorylation sites on VP22. Third, previously identified VP22-associated cellular kinase sites in HSV-1 VP22 (serines 292 and 294) were not phosphorylated in HSV-2 VP22 (serines 291 and 293). VP22 expressed alone accumulated in the cytoplasm and to a lesser extent in the nucleus. Phosphorylation by endogenous cellular kinase(s) did not alter the localization of VP22. Co-expression of HSV-2 VP22 with active UL13, but not with enzymatically inactive UL13, resulted in nuclear accumulation of VP22 and altered nuclear morphology. Surprisingly, redistribution of VP22 to the nucleus occurred independently of UL13-induced phosphorylation of VP22. The altered nuclear morphology of UL13-expressing cells was not due to apoptosis. These results demonstrate that phosphorylation of HSV-2 VP22 at multiple serine residues is induced by UL13 and cellular kinase(s), and that the nuclear/cytoplasmic distribution of VP22 is independent of its phosphorylation status but is controlled indirectly by UL13 kinase activity.},
doi = {10.1016/j.virol.2004.08.034},
url = {https://www.osti.gov/biblio/20637181}, journal = {Virology},
issn = {0042-6822},
number = 1,
volume = 330,
place = {United States},
year = {Sun Dec 05 00:00:00 EST 2004},
month = {Sun Dec 05 00:00:00 EST 2004}
}