HSV-1 ICP27 represses NF-κB activity by regulating Daxx sumoylation
Ji Ae Kim1, Mi Sun Choi1, Jung Sun Min1
1Department of Microbiology & Molecular Biology, College of Biological Science and Biotechnology, Chungnam National University, Daejeon 34134, Korea.
BMB Reports
|March 22, 2017
Summary
Herpes simplex virus type 1 ICP27 protein enhances Daxx-mediated repression of NF-κB activity. ICP27 inhibits Daxx sumoylation, leading to repression of NF-κB signaling crucial for viral replication.
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- Herpes simplex virus type 1 (HSV-1) ICP27 protein is vital for viral replication and gene expression.
- ICP27 interacts with cellular proteins, including Daxx, but the functional significance is unclear.
- Daxx is known to repress Nuclear Factor kappa B (NF-κB) activity.
Purpose of the Study:
- To investigate if ICP27 modulates Daxx's inhibitory effect on NF-κB activity.
- To elucidate the mechanism by which ICP27 influences NF-κB signaling via Daxx.
Main Methods:
- Co-immunoprecipitation to study protein interactions.
- Western blotting to assess protein modifications like sumoylation and deacetylation.
- Reporter assays to measure NF-κB transcriptional activity.
Main Results:
- ICP27 significantly enhanced Daxx-mediated repression of NF-κB activity.
- ICP27 was found to bind Daxx and inhibit Daxx sumoylation.
- ICP27 promoted Daxx-induced deacetylation of p65, a key NF-κB component.
Conclusions:
- ICP27 represses NF-κB activity by enhancing Daxx's inhibitory function.
- This repression occurs through ICP27-mediated inhibition of Daxx sumoylation and promotion of p65 deacetylation.
- The ICP27-Daxx interaction offers a novel target for controlling HSV-1 replication and associated pathologies.
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