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Herpesvirus-mediated stabilization of ICP0 expression neutralizes restriction by TRIM23
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Herpesvirus-mediated stabilization of ICP0 expression neutralizes restriction by TRIM23
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Herpesvirus-mediated stabilization of ICP0 expression neutralizes restriction by TRIM23
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Journal Article
Herpesvirus-mediated stabilization of ICP0 expression neutralizes restriction by TRIM23
2021
Overview
Herpes simplex virus (HSV) infection relies on immediate early proteins that initiate viral replication. Among them, ICP0 is known, for many years, to facilitate the onset of viral gene expression and reactivation from latency. However, how ICP0 itself is regulated remains elusive. Through genetic analyses, we identify that the viral γ₁34.5 protein, an HSV virulence factor, interacts with and prevents ICP0 from proteasomal degradation. Furthermore, we show that the host E3 ligase TRIM23, recently shown to restrict the replication of HSV-1 (and certain other viruses) by inducing autophagy, triggers the proteasomal degradation of ICP0 via K11- and K48-linked ubiquitination. Functional analyses reveal that the γ₁34.5 protein binds to and inactivates TRIM23 through blockade of K27-linked TRIM23 autoubiquitination. Deletion of γ₁34.5 or ICP0 in a recombinant HSV-1 impairs viral replication, whereas ablation of TRIM23 markedly rescues viral growth. Herein, we show that TRIM23, apart from its role in autophagy-mediated HSV-1 restriction, down-regulates ICP0, whereas viral γ₁34.5 functions to disable TRIM23. Together, these results demonstrate that posttranslational regulation of ICP0 by virus and host factors determines the outcome of HSV-1 infection.
Publisher
National Academy of Sciences
Subject
/ Animals
/ Gene Expression Regulation, Viral
/ GTP-Binding Proteins - genetics
/ GTP-Binding Proteins - metabolism
/ Herpesvirus 1, Human - physiology
/ Host-Pathogen Interactions - physiology
/ Humans
/ Immediate-Early Proteins - genetics
/ Immediate-Early Proteins - metabolism
/ Latency
/ Protein Serine-Threonine Kinases - genetics
/ Protein Serine-Threonine Kinases - metabolism
/ Proteins
/ Ubiquitin-Protein Ligases - genetics
/ Ubiquitin-Protein Ligases - metabolism
/ Viruses
