Journal
FUTURE VIROLOGY
Volume 6, Issue 4, Pages 421-429Publisher
FUTURE MEDICINE LTD
DOI: 10.2217/FVL.11.24
Keywords
E3 ubiquitin Ilgase; herpes simplex virus; ICP0; Innate immunity; intrinsic defense; nuclear domain 10; viral transactivator
Categories
Funding
- Medical Research Council - University of Glasgow Centre for Virus Research
- National Institute of Allergy and Infectious Diseases [RO1AI72357]
- Medical Research Council [MC_UP_A550_1030] Funding Source: researchfish
- MRC [MC_UP_A550_1030] Funding Source: UKRI
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Herpes simplex virus type 1 (HSV-1) has two distinct phases of its viral life cycle: lytic and latent. One viral immediate-early protein that is responsible for determining the balance between productive lytic replication and reactivation from latency is infected cell protein 0 (ICP0). ICP0 is a 775-amino acid really interesting new gene (RING)-finger-containing protein that possesses E3 ubiquitin ligase activity, which is required for ICP0 to activate HSV-1 gene expression, disrupt nuclear domain (ND) 10 structures, mediate the degradation of cellular proteins, and evade the host cell's intrinsic and innate antiviral defenses. This article examines our current understanding of ICP0's transactivating, E3 ubiquitin ligase, and antihost defense activities and their inter-relationships to one another. Lastly, we will discuss how these properties of ICP0 may be utilized as possible targets for HSV-1 antiviral therapies.
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