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Herpesviruses and the Unfolded Protein Response
Herpesviruses usurp cellular stress responses to promote viral replication and avoid immune surveillance. The unfolded protein response (UPR) is a conserved stress response that is activated when the protein load in the ER exceeds folding capacity and misfolded proteins accumulate. The UPR aims to r...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7019427/ https://www.ncbi.nlm.nih.gov/pubmed/31877732 http://dx.doi.org/10.3390/v12010017 |
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author | Johnston, Benjamin P. McCormick, Craig |
author_facet | Johnston, Benjamin P. McCormick, Craig |
author_sort | Johnston, Benjamin P. |
collection | PubMed |
description | Herpesviruses usurp cellular stress responses to promote viral replication and avoid immune surveillance. The unfolded protein response (UPR) is a conserved stress response that is activated when the protein load in the ER exceeds folding capacity and misfolded proteins accumulate. The UPR aims to restore protein homeostasis through translational and transcriptional reprogramming; if homeostasis cannot be restored, the UPR switches from “helper” to “executioner”, triggering apoptosis. It is thought that the burst of herpesvirus glycoprotein synthesis during lytic replication causes ER stress, and that these viruses may have evolved mechanisms to manage UPR signaling to create an optimal niche for replication. The past decade has seen considerable progress in understanding how herpesviruses reprogram the UPR. Here we provide an overview of the molecular events of UPR activation, signaling and transcriptional outputs, and highlight key evidence that herpesviruses hijack the UPR to aid infection. |
format | Online Article Text |
id | pubmed-7019427 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-70194272020-03-09 Herpesviruses and the Unfolded Protein Response Johnston, Benjamin P. McCormick, Craig Viruses Review Herpesviruses usurp cellular stress responses to promote viral replication and avoid immune surveillance. The unfolded protein response (UPR) is a conserved stress response that is activated when the protein load in the ER exceeds folding capacity and misfolded proteins accumulate. The UPR aims to restore protein homeostasis through translational and transcriptional reprogramming; if homeostasis cannot be restored, the UPR switches from “helper” to “executioner”, triggering apoptosis. It is thought that the burst of herpesvirus glycoprotein synthesis during lytic replication causes ER stress, and that these viruses may have evolved mechanisms to manage UPR signaling to create an optimal niche for replication. The past decade has seen considerable progress in understanding how herpesviruses reprogram the UPR. Here we provide an overview of the molecular events of UPR activation, signaling and transcriptional outputs, and highlight key evidence that herpesviruses hijack the UPR to aid infection. MDPI 2019-12-21 /pmc/articles/PMC7019427/ /pubmed/31877732 http://dx.doi.org/10.3390/v12010017 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Johnston, Benjamin P. McCormick, Craig Herpesviruses and the Unfolded Protein Response |
title | Herpesviruses and the Unfolded Protein Response |
title_full | Herpesviruses and the Unfolded Protein Response |
title_fullStr | Herpesviruses and the Unfolded Protein Response |
title_full_unstemmed | Herpesviruses and the Unfolded Protein Response |
title_short | Herpesviruses and the Unfolded Protein Response |
title_sort | herpesviruses and the unfolded protein response |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7019427/ https://www.ncbi.nlm.nih.gov/pubmed/31877732 http://dx.doi.org/10.3390/v12010017 |
work_keys_str_mv | AT johnstonbenjaminp herpesvirusesandtheunfoldedproteinresponse AT mccormickcraig herpesvirusesandtheunfoldedproteinresponse |