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Updated: May 11, 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

The interaction of the cellular export adaptor protein Aly/REF with ICP27 contributes to the efficiency of herpes

Xiaochen Tian1, Gayathri Devi-Rao, Alexander P Golovanov

  • 1Department of Microbiology and Molecular Genetics, University of California, Irvine, Irvine, California, USA.

Journal of Virology
|May 3, 2013
PubMed

Insights

The interaction between Herpes simplex virus 1 (HSV-1) protein ICP27 and Aly/REF is crucial for efficient viral mRNA export. Mutating key residues in ICP27 significantly reduced virus production and mRNA export.

Area of Science:

  • Virology
  • Molecular Biology
  • Cellular Biology

Background:

  • Herpes simplex virus 1 (HSV-1) protein ICP27 facilitates viral mRNA export by interacting with cellular export factors.
  • ICP27 links viral mRNAs to the cellular mRNA export pathway via TAP/NXF and Aly/REF.
  • Previous studies suggested Aly/REF might be dispensable for viral RNA export.

Purpose of the Study:

  • To investigate the role of the ICP27-Aly/REF interaction in viral mRNA export during HSV-1 infection.
  • To determine the functional significance of specific ICP27 residues (W105, R107, L108) that interface with Aly/REF.

Main Methods:

  • Site-directed mutagenesis was used to alter ICP27 residues W105, R107, and L108 to alanine.
  • A recombinant HSV-1 virus (WRL-A) carrying these mutations was constructed.
  • Viral production and mRNA export efficiency were assessed during infection with the WRL-A virus.

Main Results:

  • Virus production was reduced approximately 10-fold in infections with the WRL-A mutant virus.
  • The export of ICP27 protein and most viral mRNAs was significantly less efficient in WRL-A infected cells.
  • The structural interaction interface between ICP27 and Aly/REF is critical for efficient viral mRNA export.

Conclusions:

  • The interaction between HSV-1 ICP27 and the cellular export factor Aly/REF significantly contributes to efficient viral mRNA export.
  • Disruption of the ICP27-Aly/REF interaction impairs viral replication and mRNA export pathways.
  • This interaction represents a key mechanism exploited by HSV-1 for its life cycle.

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