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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| Format: | Article |
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Frontiers Media S.A.
2023-06-01
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| Series: | Frontiers in Cellular and Infection Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fcimb.2023.1217383/full |
| _version_ | 1797808366179844096 |
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| author | Mingjiu Zhao Mengdi Zhang Zhou Yang Zhiguang Zhou Jiaqi Huang Jiaqi Huang Bin Zhao Bin Zhao |
| author_facet | Mingjiu Zhao Mengdi Zhang Zhou Yang Zhiguang Zhou Jiaqi Huang Jiaqi Huang Bin Zhao Bin Zhao |
| author_sort | Mingjiu Zhao |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-13T06:36:28Z |
| format | Article |
| id | doaj.art-dc3fcb4efaa8441c98a3d1801ac3a6fc |
| institution | Directory Open Access Journal |
| issn | 2235-2988 |
| language | English |
| last_indexed | 2024-03-13T06:36:28Z |
| publishDate | 2023-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj.art-dc3fcb4efaa8441c98a3d1801ac3a6fc2023-06-09T05:10:12ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882023-06-011310.3389/fcimb.2023.12173831217383Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infectionMingjiu Zhao0Mengdi Zhang1Zhou Yang2Zhiguang Zhou3Jiaqi Huang4Jiaqi Huang5Bin Zhao6Bin Zhao7National Clinical Research Center for Metabolic Diseases, Metabolic Syndrome Research Center, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, The Second Xiangya Hospital of Central South University, Changsha, Hunan, ChinaNational Clinical Research Center for Metabolic Diseases, Metabolic Syndrome Research Center, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, The Second Xiangya Hospital of Central South University, Changsha, Hunan, ChinaNational Clinical Research Center for Metabolic Diseases, Metabolic Syndrome Research Center, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, The Second Xiangya Hospital of Central South University, Changsha, Hunan, ChinaNational Clinical Research Center for Metabolic Diseases, Metabolic Syndrome Research Center, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, The Second Xiangya Hospital of Central South University, Changsha, Hunan, ChinaNational Clinical Research Center for Metabolic Diseases, Metabolic Syndrome Research Center, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, The Second Xiangya Hospital of Central South University, Changsha, Hunan, ChinaXiangya School of Public Health, Central South University, Changsha, ChinaNational Clinical Research Center for Metabolic Diseases, Metabolic Syndrome Research Center, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, The Second Xiangya Hospital of Central South University, Changsha, Hunan, ChinaFurong Laboratory, Central South University, Changsha, ChinaEver 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.https://www.frontiersin.org/articles/10.3389/fcimb.2023.1217383/fullubiquitinE3 ubiquitin ligasesdeubiquitinating enzymes (DUBs)SARS-CoV-2COVID-19 |
| spellingShingle | Mingjiu Zhao Mengdi Zhang Zhou Yang Zhiguang Zhou Jiaqi Huang Jiaqi Huang Bin Zhao Bin Zhao Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection Frontiers in Cellular and Infection Microbiology ubiquitin E3 ubiquitin ligases deubiquitinating enzymes (DUBs) SARS-CoV-2 COVID-19 |
| 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 | ubiquitin E3 ubiquitin ligases deubiquitinating enzymes (DUBs) SARS-CoV-2 COVID-19 |
| url | https://www.frontiersin.org/articles/10.3389/fcimb.2023.1217383/full |
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