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Related Experiment Videos

Phosphorylation site mutations affect herpes simplex virus type 1 ICP0 function.

David J Davido1, William F von Zagorski, William S Lane

  • 1Beth Israel Deaconess Medical Center, 330 Brookline Ave., RN 123, Boston, MA 02215, USA.

Journal of Virology
|December 23, 2004
PubMed
Summary
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Phosphorylation regulates the function of herpes simplex virus type 1 (HSV-1) infected-cell protein 0 (ICP0). Mutating phosphorylation sites altered ICP0

Area of Science:

  • Virology
  • Molecular Biology
  • Cellular Biology

Background:

  • Herpes simplex virus type 1 (HSV-1) immediate-early (IE) regulatory protein infected-cell protein 0 (ICP0) is a potent transactivator of viral and cellular genes.
  • Previous studies indicated ICP0 is highly phosphorylated, suggesting phosphorylation may influence its activity.

Purpose of the Study:

  • To investigate the role of ICP0 phosphorylation in regulating its functions.
  • To identify specific phosphorylation sites within ICP0 and assess their impact on viral gene regulation and replication.

Main Methods:

  • ICP0 was purified and phosphorylation sites were mapped using microcapillary high-pressure liquid chromatography tandem mass spectrometry.
  • Site-directed mutagenesis was employed to create mutant ICP0 forms (Phos 1, Phos 2, Phos 3) with altered phosphorylation sites.

Related Experiment Videos

  • Functional assays evaluated the effects of these mutations on ICP0's localization, interaction with PML protein, transactivation, and viral replication complementation.

    • Main Results:

    • Three phosphorylated regions with 11 putative sites, crucial for transactivation, were identified in ICP0.
    • Mutations in these sites altered ICP0's subcellular localization, PML-associated nuclear domain 10 (ND10) staining pattern, and transactivating activity.
    • Only mutations in the Phos 1 region significantly impaired ICP0's ability to complement HSV-1 replication in ICP0 null mutants.

    Conclusions:

    • Phosphorylation is a critical regulatory mechanism for ICP0 function.
    • Specific phosphorylation sites within ICP0 modulate its localization, transactivation capabilities, and essential role in viral replication.