Related Experiment Video

Updated: Jun 12, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
06:40

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy

Published on: November 4, 2018

ICP0 dismantles microtubule networks in herpes simplex virus-infected cells

Mingyu Liu1, Edward E Schmidt, William P Halford

  • 1Department of Microbiology and Immunology, Southern Illinois University School of Medicine, Springfield, Illinois, USA.

Plos One
|June 15, 2010
PubMed

Insights

Herpes simplex virus protein ICP0, an E3 ligase, unexpectedly moves to the cytoplasm to dismantle host cell microtubules. This viral protein regulates microtubule stability, impacting the virus life cycle.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Infected-cell protein 0 (ICP0) is a key regulator of herpes simplex virus (HSV) replication and latency.
  • ICP0's nuclear functions have been extensively studied for decades.
  • The precise mechanism of ICP0's action, particularly its localization and cellular interactions, remains incompletely understood.

Purpose of the Study:

  • To investigate the subcellular localization and function of ICP0 during HSV infection.
  • To elucidate the role of ICP0 in host cell manipulation beyond its known nuclear functions.
  • To identify novel mechanisms by which HSV controls host cell processes.

Main Methods:

  • Construction of HSV-1 viruses expressing GFP-tagged ICP0 for visualization.
  • Microscopy to determine ICP0 localization in infected cells.
  • Analysis of microtubule network integrity in infected and transfected cells.
  • Utilizing a RING finger mutant of ICP0 to assess its enzymatic activity's role.

Main Results:

  • Both GFP-tagged and wild-type ICP0 were predominantly found in the cytoplasm of HSV-infected cells, contrary to prior assumptions.
  • ICP0 translocated from the nucleus to the cytoplasm during the early phase of infection.
  • ICP0 actively dismantled the host cell's microtubule network, a previously unrecognized function.
  • A RING finger mutant of ICP0 could bundle but not disperse microtubules, highlighting the importance of its E3 ligase activity.

Conclusions:

  • ICP0 plays a dual role in the HSV life cycle: nuclear regulation of viral mRNA and cytoplasmic disruption of microtubules.
  • ICP0 is the first reported viral E3 ligase that actively regulates microtubule stability.
  • The dismantling of the microtubule network by ICP0 likely facilitates virion synthesis and/or egress.
  • This finding offers new insights into viral strategies for manipulating host cell infrastructure.

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