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Updated: Jun 15, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
Published on: November 4, 2018
SR proteins SRp20 and 9G8 contribute to efficient export of herpes simplex virus 1 mRNAs
Laurimar Escudero-Paunetto1, Ling Li, Felicia P Hernandez
1Department of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, CA 92697, USA.
Abstract:
Herpes simplex virus 1 (HSV-1) mRNAs are exported to the cytoplasm through the export receptor TAP/NFX1. HSV-1 multifunctional protein ICP27 interacts with TAP/NXF1, binds viral RNAs, and is required for efficient viral RNA export. In ICP27 mutant infections, viral RNA export is reduced but not ablated, indicating that other export adaptors can aid in viral RNA export. Export adaptor protein Aly/REF is recruited to viral replication compartments, however, Aly/REF knockdown has little effect on viral RNA export. SR proteins SRp20 and 9G8 interact with TAP/NXF1 and mediate export of some cellular RNAs. We report that siRNA knockdown of SRp20 or 9G8 resulted in about a 10 fold decrease in virus yields and in nuclear accumulation of polyA+ RNA. In infected cells depleted of SRp20, newly transcribed Bromouridine-labeled RNA also accumulated in the nucleus. We conclude that SRp20 and 9G8 contribute to HSV-1 RNA export.
Insights
SR proteins SRp20 and 9G8 are crucial for efficient Herpes simplex virus 1 (HSV-1) RNA export. Depleting these SR proteins significantly reduces virus yield and causes RNA to accumulate in the nucleus.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Herpes simplex virus 1 (HSV-1) requires efficient mRNA export for replication.
- The TAP/NXF1 receptor mediates viral RNA export, with ICP27 playing a key role.
- Other export adaptors like Aly/REF have limited impact on HSV-1 RNA export.
Purpose of the Study:
- To investigate the role of SR proteins SRp20 and 9G8 in HSV-1 RNA export.
- To determine if SR proteins contribute to viral RNA export pathways beyond ICP27.
Main Methods:
- Small interfering RNA (siRNA) knockdown of SRp20 and 9G8 in HSV-1 infected cells.
- Analysis of viral RNA export efficiency via nuclear accumulation of polyadenylated (polyA+) RNA.
- Tracking of newly transcribed RNA using Bromouridine labeling in SRp20-depleted cells.
Main Results:
- siRNA knockdown of SRp20 or 9G8 led to a tenfold decrease in HSV-1 virus yields.
- Depletion of SRp20 or 9G8 resulted in significant nuclear accumulation of polyA+ RNA.
- In SRp20-depleted cells, newly transcribed RNA accumulated in the nucleus, indicating impaired export.
Conclusions:
- SR proteins SRp20 and 9G8 are essential for efficient HSV-1 RNA export.
- These SR proteins play a significant role in facilitating the transport of viral RNA to the cytoplasm.
- The findings suggest a novel mechanism for viral RNA export involving SR proteins.
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