Related Experiment Video
Updated: May 24, 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
Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host
Poonam Malik1, Alijan Tabarraei, Ralph H Kehlenbach
1Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, Scotland, United Kingdom. p.malik@ed.ac.uk
Abstract:
The herpes simplex virus ICP27 protein is important for the expression and nuclear export of viral mRNAs. Although several binding sites have been mapped along the ICP27 sequence for various RNA and protein partners, including the transport receptor TAP of the host cell nuclear transport machinery, several aspects of ICP27 trafficking through the nuclear pore complex remain unclear. We investigated if ICP27 could interact directly with the nuclear pore complex itself, finding that ICP27 directly binds the core nucleoporin Nup62. This is confirmed through co-immunoprecipitation and in vitro binding assays with purified components. Mapping with ICP27 deletion and point mutants further shows that the interaction requires sequences in both the N and C termini of ICP27. Expression of wild type ICP27 protein inhibited both classical, importin α/β-dependent and transportin-dependent nuclear import. In contrast, an ICP27 point mutant that does not interact with Nup62 had no such inhibitory effect. We suggest that ICP27 association with Nup62 provides additional binding sites at the nuclear pore for ICP27 shuttling, thus supporting ICP27-mediated transport. We propose that ICP27 competes with some host cell transport receptors for binding, resulting in inhibition of those host transport pathways.
Insights
Herpes simplex virus ICP27 protein binds Nup62, a nuclear pore component. This interaction influences viral mRNA export and host cell nuclear import pathways.
Area of Science:
- Molecular Biology
- Virology
- Cell Biology
Background:
- The herpes simplex virus ICP27 protein is crucial for viral gene expression and mRNA nuclear export.
- While ICP27's interactions with RNA and host transport factors like TAP are known, its direct interaction with the nuclear pore complex (NPC) is not fully understood.
Purpose of the Study:
- To investigate the direct interaction between the herpes simplex virus ICP27 protein and the nuclear pore complex.
- To elucidate the role of ICP27's interaction with nucleoporins in viral nuclear export and host nuclear transport.
Main Methods:
- Co-immunoprecipitation assays to detect protein-protein interactions.
- In vitro binding assays using purified proteins.
- Analysis of ICP27 deletion and point mutants to map interaction domains.
Main Results:
- ICP27 directly binds to Nup62, a core nucleoporin of the nuclear pore complex.
- The interaction between ICP27 and Nup62 requires sequences in both the N- and C-termini of ICP27.
- Wild-type ICP27 expression inhibits importin α/β- and transportin-dependent nuclear import, while an Nup62-binding deficient mutant does not.
Conclusions:
- ICP27's association with Nup62 facilitates its own nuclear transport and viral mRNA export.
- ICP27 may inhibit host cell nuclear import by competing with host transport receptors for binding to NPCs.
Related Concept Videos
Regulation of Nuclear Protein Sorting
Nuclear Protein Sorting
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Nuclear Export
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Nuclear Localization Signals and Import
Inhibitors of Viral Protein Synthesis
Nuclear Export of mRNA

