casein-kinase-ii and Herpes-Simplex

casein-kinase-ii has been researched along with Herpes-Simplex* in 2 studies

Other Studies

2 other study(ies) available for casein-kinase-ii and Herpes-Simplex

ArticleYear
Casein kinase II controls TBK1/IRF3 activation in IFN response against viral infection.
    Journal of immunology (Baltimore, Md. : 1950), 2015, May-01, Volume: 194, Issue:9

    By sensing viral nucleic acids, host innate receptors elicit signaling pathways converging on TBK1-IFN regulatory factor (IRF)3 axis in mediating IFN-αβ induction and defense mechanisms. In contrast, viruses have evolved with diverse immune evasion/interference mechanisms to undermine innate receptor signaling and IFN response. In this regard, approaches enabling host to overcome such immune evasion/interference mechanisms are urgently needed to combat infections by epidemic/pandemic viruses. In this study, we report that protein kinase CK2 serves as a key component controlling TBK1 and IRF3 activation in IFN-inducing TLR, RIG-I-like receptors, and cGAS/STING signaling pathways. Accordingly, knocking down of CK2 expression or genetic ablation of its kinase activity resulted in elevated IFN-αβ response in response to infection by DNA and RNA viruses. Moreover, PP2A was identified as one of the intermediate phosphatases responsible for CK2-regulated IFN response, suggesting that CK2 may regulate TBK1 and IRF3 activation indirectly. Importantly, blockade of CK2 activity by small molecule inhibitor was able to activate TBK1, whereby eliciting effective host defense mechanisms against hepatitis C virus infection. Taken together, our results identify CK2 as a novel regulator of TBK1 and IRF3 and suggest that targeting CK2 by small molecular inhibitor may be a viable approach to prevent and treat viral infections.

    Topics: Animals; Casein Kinase II; Cell Line; Disease Models, Animal; Hepatitis C; Herpes Simplex; Herpesvirus 1, Human; Humans; Interferon Regulatory Factor-3; Interferons; Membrane Proteins; Mice; Protein Serine-Threonine Kinases; Toll-Like Receptor 3; Toll-Like Receptor 4; Virus Diseases

2015
CK2 inhibitors increase the sensitivity of HSV-1 to interferon-β.
    Antiviral research, 2011, Volume: 91, Issue:3

    Herpes simplex virus type 1 (HSV-1) requires the activities of cellular kinases for efficient replication. The host kinase, CK2, has been shown or is predicted to modify several HSV-1 proteins and has been proposed to affect one or more steps in the viral life cycle. Furthermore, potential cellular and viral substrates of CK2 are involved in antiviral pathways and viral counter-defenses, respectively, suggesting that CK2 regulates these processes. Consequently, we tested whether pharmacological inhibitors of CK2 impaired HSV-1 replication, either alone or in combination with the cellular antiviral factor, interferon-β (IFN-β). Our results indicate that the use of CK2 inhibitors results in a minor reduction in HSV-1 replication but enhanced the inhibitory effect of IFN-β on replication. This effect was dependent on the HSV-1 E3 ubiquitin ligase, infected cell protein 0 (ICP0), which impairs several host antiviral responses, including that produced by IFN-β. Inhibitors of CK2 did not, however, impede the ability of ICP0 to induce the degradation of two cellular targets: the promyelocytic leukemia protein (PML) and the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). Notably, this effect was only apparent for HSV-1, as the CK2 inhibitors did not enhance the antiviral effect of IFN-β on either vesicular stomatitis virus or adenovirus type 5. Thus, our data suggest that the activity of CK2 is required for an early function during viral infection that assists the growth of HSV-1 in IFN-β-treated cells.

    Topics: Adenoviridae; Antiviral Agents; Blotting, Western; Casein Kinase II; Cell Line; Herpes Simplex; Herpesvirus 1, Human; Host-Pathogen Interactions; Humans; Immediate-Early Proteins; Interferon-beta; Lung; Microscopy, Fluorescence; Protein Kinase Inhibitors; Signal Transduction; Ubiquitin-Protein Ligases; Vesiculovirus; Virus Replication

2011