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VZV ORF47 Serine Protein Kinase and Its Viral Substrates

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Varicella-zoster Virus

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 342))

Abstract

ORF47, a serine protein kinase of varicella-zoster virus (VZV) and homolog of herpes simplex virus UL13, is an interesting modulator of VZV pathogenesis. This chapter summarizes research showing that ORF47 protein kinase activity, by virtue of phosphorylation of or binding to various viral substrates, regulates VZV proteins during all phases of viral infection and has a pronounced effect on the trafficking of gE, the predominant VZV glycoprotein, which in turn is critical for cell-to-cell spread of the virus. Casein kinase II, an ubiquitous cellular protein kinase, recognizes a similar but less stringent phosphorylation consensus sequence and can partially compensate for lack of ORF47 activity in VZV-infected cells. Differences between the phosphorylation consensus sites of the viral and cellular kinases are outlined in detail.

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Authors and Affiliations

  1. Department of Pediatrics/2501 JCP, University of Iowa Hospital, Iowa City, IA, 52242, USA

    Teri K. Kenyon & Charles Grose

Authors
  1. Teri K. Kenyon
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  2. Charles Grose
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Corresponding author

Correspondence to Charles Grose .

Editor information

Editors and Affiliations

  1. Department of Infectious Diseases and Im, Head, VZV Research Laboratory, University of Sydney, Room 601 Blackburn Building D06, Sydney, 2006, New South Wales, Australia

    Allison Abendroth

  2. School of Medicine, Dept. Microbiology & Immunology, Stanford University, Pasteur Drive 300, Stanford, 94305-5124, California, USA

    Ann M. Arvin

  3. 2215 Weiskotten Hall, Upstate Medical University, East Adams Street 750, Syracuse, 13210, New York, USA

    Jennifer F. Moffat

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Kenyon, T.K., Grose, C. (2010). VZV ORF47 Serine Protein Kinase and Its Viral Substrates. In: Abendroth, A., Arvin, A., Moffat, J. (eds) Varicella-zoster Virus. Current Topics in Microbiology and Immunology, vol 342. Springer, Berlin, Heidelberg. https://doi.org/10.1007/82_2009_5

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