HSV-1 ICP27 suppresses NF-κB activity by stabilizing IκBα

Abstract

Nuclear factor κB (NF-κB) is associated with the transcriptional activation of genes encoding chemokines, adhesion molecules, cytokines, and anti-apoptotic proteins, which are key components in immune responses and viral infection. Many viruses modulate NF-κB through numerous viral gene products to allow productive infections and immune escape. Here we report that herpes simplex virus-1 infected cell protein 27 (HSV-1 ICP27), an immediate early protein of HSV-1, represses NF-κB activity through binding to inhibitor of κB (IκBα), blocking phosphorylation and ubiquitination of IκBα, and stabilizing IκBα. These data may explain how NF-κB activity is regulated by ICP27 to escape immune responses during the very early period of HSV-1 infection. Structured summary: MINT-6549405:IkappaBalpha (uniprotkb:P25963) physically interacts (MI:0218) with ICP27 (uniprotkb:Q9J0X9) by anti bait coimmunoprecipitation (MI:0006)MINT-6549385:IkappaBalpha (uniprotkb:P25963)physically interacts (MI:0218) with ICP27 (uniprotkb:Q9J0X9) by anti tag coimmunoprecipitation (MI:0007)MINT-6549372:IkappaBalpha (uniprotkb:P25963) physically interacts (MI:0218) with ICP27 (uniprotkb:Q9J0X9) by pull down (MI:0096). © 2008 Federation of European Biochemical Societies.