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HSV-1 ICP0: An E3 Ubiquitin Ligase That Counteracts Host Intrinsic and Innate Immunity
Lanfranca, Mirna Perusina Mostafa, Heba H. Davido, David J.
Lanfranca, Mirna Perusina
Mostafa, Heba H.
Davido, David J.
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Abstract
The herpes simplex virus type 1 (HSV-1) encoded E3 ubiquitin ligase, infected
cell protein 0 (ICP0), is required for efficient lytic viral replication and regulates the switch
between the lytic and latent states of HSV-1. As an E3 ubiquitin ligase, ICP0 directs the
proteasomal degradation of several cellular targets, allowing the virus to counteract
different cellular intrinsic and innate immune responses. In this review, we will focus on
how ICP0’s E3 ubiquitin ligase activity inactivates the host intrinsic defenses, such as nuclear domain 10 (ND10), SUMO, and the DNA damage response to HSV-1 infection. In
addition, we will examine ICP0’s capacity to impair the activation of interferon (innate)
regulatory mediators that include IFI16 (IFN γ-inducible protein 16), MyD88 (myeloid
differentiation factor 88), and Mal (MyD88 adaptor-like protein). We will also consider
how ICP0 allows HSV-1 to evade activation of the NF-κB (nuclear factor kappa B)
inflammatory signaling pathway. Finally, ICP0’s paradoxical relationship with USP7
(ubiquitin specific protease 7) and its roles in intrinsic and innate immune responses to
HSV-1 infection will be discussed.
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This is an Open Access article distributed under the terms of the Open Access Policy.
Date
2014-05-20
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MDPI
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Keywords
Herpes simplex virus, HSV, E3 ubiquitin ligase, Infected cell protein 0, ICP0, Intrinsic immunity, Innate immunity
Citation
Lanfranca, Mirna Perusina, Mostafa Heba H., Davido, David J. "HSV-1 ICP0: An E3 Ubiquitin Ligase That Counteracts Host Intrinsic and Innate Immunity." MDPI. May 20, 2014.