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Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection

Ever since its emergence in 2019, COVID-19 has rapidly disseminated worldwide, engendering a pervasive pandemic that has profoundly impacted healthcare systems and the socio-economic milieu. A plethora of studies has been conducted targeting its pathogenic virus, SARS-CoV-2, to find ways to combat C...

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Autores principales: Zhao, Mingjiu, Zhang, Mengdi, Yang, Zhou, Zhou, Zhiguang, Huang, Jiaqi, Zhao, Bin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10288995/
https://www.ncbi.nlm.nih.gov/pubmed/37360529
http://dx.doi.org/10.3389/fcimb.2023.1217383
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author Zhao, Mingjiu
Zhang, Mengdi
Yang, Zhou
Zhou, Zhiguang
Huang, Jiaqi
Zhao, Bin
author_facet Zhao, Mingjiu
Zhang, Mengdi
Yang, Zhou
Zhou, Zhiguang
Huang, Jiaqi
Zhao, Bin
author_sort Zhao, Mingjiu
collection PubMed
description Ever since its emergence in 2019, COVID-19 has rapidly disseminated worldwide, engendering a pervasive pandemic that has profoundly impacted healthcare systems and the socio-economic milieu. A plethora of studies has been conducted targeting its pathogenic virus, SARS-CoV-2, to find ways to combat COVID-19. The ubiquitin-proteasome system (UPS) is widely recognized as a crucial mechanism that regulates human biological activities by maintaining protein homeostasis. Within the UPS, the ubiquitination and deubiquitination, two reversible modifications, of substrate proteins have been extensively studied and implicated in the pathogenesis of SARS-CoV-2. The regulation of E3 ubiquitin ligases and DUBs(Deubiquitinating enzymes), which are key enzymes involved in the two modification processes, determines the fate of substrate proteins. Proteins associated with the pathogenesis of SARS-CoV-2 may be retained, degraded, or even activated, thus affecting the ultimate outcome of the confrontation between SARS-CoV-2 and the host. In other words, the clash between SARS-CoV-2 and the host can be viewed as a battle for dominance over E3 ubiquitin ligases and DUBs, from the standpoint of ubiquitin modification regulation. This review primarily aims to clarify the mechanisms by which the virus utilizes host E3 ubiquitin ligases and DUBs, along with its own viral proteins that have similar enzyme activities, to facilitate invasion, replication, escape, and inflammation. We believe that gaining a better understanding of the role of E3 ubiquitin ligases and DUBs in COVID-19 can offer novel and valuable insights for developing antiviral therapies.
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spelling pubmed-102889952023-06-24 Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection Zhao, Mingjiu Zhang, Mengdi Yang, Zhou Zhou, Zhiguang Huang, Jiaqi Zhao, Bin Front Cell Infect Microbiol Cellular and Infection Microbiology Ever since its emergence in 2019, COVID-19 has rapidly disseminated worldwide, engendering a pervasive pandemic that has profoundly impacted healthcare systems and the socio-economic milieu. A plethora of studies has been conducted targeting its pathogenic virus, SARS-CoV-2, to find ways to combat COVID-19. The ubiquitin-proteasome system (UPS) is widely recognized as a crucial mechanism that regulates human biological activities by maintaining protein homeostasis. Within the UPS, the ubiquitination and deubiquitination, two reversible modifications, of substrate proteins have been extensively studied and implicated in the pathogenesis of SARS-CoV-2. The regulation of E3 ubiquitin ligases and DUBs(Deubiquitinating enzymes), which are key enzymes involved in the two modification processes, determines the fate of substrate proteins. Proteins associated with the pathogenesis of SARS-CoV-2 may be retained, degraded, or even activated, thus affecting the ultimate outcome of the confrontation between SARS-CoV-2 and the host. In other words, the clash between SARS-CoV-2 and the host can be viewed as a battle for dominance over E3 ubiquitin ligases and DUBs, from the standpoint of ubiquitin modification regulation. This review primarily aims to clarify the mechanisms by which the virus utilizes host E3 ubiquitin ligases and DUBs, along with its own viral proteins that have similar enzyme activities, to facilitate invasion, replication, escape, and inflammation. We believe that gaining a better understanding of the role of E3 ubiquitin ligases and DUBs in COVID-19 can offer novel and valuable insights for developing antiviral therapies. Frontiers Media S.A. 2023-06-09 /pmc/articles/PMC10288995/ /pubmed/37360529 http://dx.doi.org/10.3389/fcimb.2023.1217383 Text en Copyright © 2023 Zhao, Zhang, Yang, Zhou, Huang and Zhao https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cellular and Infection Microbiology
Zhao, Mingjiu
Zhang, Mengdi
Yang, Zhou
Zhou, Zhiguang
Huang, Jiaqi
Zhao, Bin
Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection
title Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection
title_full Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection
title_fullStr Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection
title_full_unstemmed Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection
title_short Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection
title_sort role of e3 ubiquitin ligases and deubiquitinating enzymes in sars-cov-2 infection
topic Cellular and Infection Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10288995/
https://www.ncbi.nlm.nih.gov/pubmed/37360529
http://dx.doi.org/10.3389/fcimb.2023.1217383
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