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Viruses
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Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023
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Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Human Virology and Viral Diseases".

Deadline for manuscript submissions: closed (28 February 2023) | Viewed by 12671

Special Issue Editor

Dr. Elana Ehrlich

E-Mail Website
Guest Editor
Department of Biological Sciences, Towson University, Towson, MD 21252, USA
Interests: herpesviruses; ubiquitin proteasome system; host pathogen interactions; post-translational modifications

Special Issue Information

Dear Colleagues,

Viruses are master manipulators of cell biology often hijacking the ubiquitin and ubiquitin-like (Ubl) systems of post-translational modifications to evade host defenses and promote replication success. Much can be learned about the requirements for productive viral replication through the identification and characterization of targets of ubiquitin and Ubl modification.

In this Special Issue, we aim to compile reports and reviews focused on the following research areas:

  • Diverse viral ubiquitin ligases and deubiquitinases;
  • SUMO targeting ubiquitin ligases;
  • Viral proteins that co-opt or modify cellular the ubiquitin proteasome system;
  • Omics-based approaches to characterizing the viral ubiquitin or Ubl modified proteome;
  • Additional viral mechanisms that target the ubiquitin proteasome system, Ubls, and autophagy.

Dr. Elana Ehrlich
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • ubiquitin
  • SUMO
  • Ubl
  • ubiquitin ligase
  • DUB
 

Published Papers (7 papers)

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Research

Jump to: Review

18 pages, 5467 KiB  
Article
All-trans Retinoic Acid Inhibits Hepatitis B Virus Replication by Downregulating HBx Levels via Siah-1-Mediated Proteasomal Degradation
by Jiwoo Han and Kyung Lib Jang
Viruses 2023, 15(7), 1456; https://doi.org/10.3390/v15071456 - 27 Jun 2023
Cited by 2 | Viewed by 1347
Abstract
All-trans retinoic acid (ATRA), the most biologically active metabolite of vitamin A, is known to abolish the potential of HBx to downregulate the levels of p14, p16, and p21 and to stimulate cell growth during hepatitis B virus (HBV) infection, contributing to [...] Read more.
All-trans retinoic acid (ATRA), the most biologically active metabolite of vitamin A, is known to abolish the potential of HBx to downregulate the levels of p14, p16, and p21 and to stimulate cell growth during hepatitis B virus (HBV) infection, contributing to its chemopreventive and therapeutic effects against HBV-associated hepatocellular carcinoma. Here, we demonstrated that ATRA antagonizes HBx to inhibit HBV replication. For this effect, ATRA individually or in combination with HBx upregulated p53 levels, resulting in upregulation of seven in absentia homolog 1 (Siah-1) levels. Siah-1, an E3 ligase, induces ubiquitination and proteasomal degradation of HBx in the presence of ATRA. The ability of ATRA to induce Siah-1-mediated HBx degradation and the subsequent inhibition of HBV replication was proven in an in vitro HBV replication model. The effects of ATRA became invalid when either p53 or Siah-1 was knocked down by a specific shRNA, providing direct evidence for the role of p53 and Siah-1 in the negative regulation of HBV replication by ATRA. Full article
(This article belongs to the Special Issue Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023)
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21 pages, 3776 KiB  
Article
Tumor Suppressor p53 Inhibits Hepatitis B Virus Replication by Downregulating HBx via E6AP-Mediated Proteasomal Degradation in Human Hepatocellular Carcinoma Cell Lines
by Ha-Yeon Lim, Jiwoo Han, Hyunyoung Yoon and Kyung Lib Jang
Viruses 2022, 14(10), 2313; https://doi.org/10.3390/v14102313 - 21 Oct 2022
Cited by 6 | Viewed by 2402
Abstract
HBx, a multifunctional regulatory protein, plays an essential role in the replication and pathogenesis of the hepatitis B virus (HBV). In this study, we found that in human hepatoma cells, the tumor suppressor p53 downregulates HBx via ubiquitin-dependent proteasomal degradation. p53 transcriptional activity [...] Read more.
HBx, a multifunctional regulatory protein, plays an essential role in the replication and pathogenesis of the hepatitis B virus (HBV). In this study, we found that in human hepatoma cells, the tumor suppressor p53 downregulates HBx via ubiquitin-dependent proteasomal degradation. p53 transcriptional activity that results from HBV infection was not essential for this effect. This was shown by treatment with a potent p53 inhibitor, pifithrin-α. Instead, we found that p53 facilitated the binding of E6-associated protein (E6AP), which is an E3 ligase, to HBx and induced E6AP-mediated HBx ubiquitination in a ternary complex of p53, E6AP, and HBx. The ability of p53 to induce E6AP-mediated downregulation of HBx and inhibit HBV replication was demonstrated in an in vitro HBV infection system. This study may provide insights into the regulation of HBx and HBV replication, especially with respect to p53 status, which may also help in understanding HBV-associated tumorigenesis in patients. Full article
(This article belongs to the Special Issue Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023)
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12 pages, 2481 KiB  
Article
Hazara Orthonairovirus Nucleoprotein Antagonizes Type I Interferon Production by Inhibition of RIG-I Ubiquitination
by Keisuke Ohta, Naoki Saka and Machiko Nishio
Viruses 2022, 14(9), 1965; https://doi.org/10.3390/v14091965 - 4 Sep 2022
Cited by 3 | Viewed by 1654
Abstract
Viruses have evolved various strategies to evade the host innate immune system. The relationship between nairoviruses and the interferon (IFN) system is poorly understood. We investigated whether and how nairoviruses antagonize host innate immunity using Hazara orthonairovirus (HAZV) as a surrogate model for [...] Read more.
Viruses have evolved various strategies to evade the host innate immune system. The relationship between nairoviruses and the interferon (IFN) system is poorly understood. We investigated whether and how nairoviruses antagonize host innate immunity using Hazara orthonairovirus (HAZV) as a surrogate model for Crimean-Congo hemorrhagic fever virus. HAZV nucleoprotein (N) was found to interact with the tripartite motif-containing protein 25 (TRIM25). The N-terminal region of N protein and the C-terminal region of TRIM25 are important for their interaction. Overexpression of N protein results in weakened interaction of TRIM25 with retinoic acid-inducible gene I (RIG-I). Furthermore, K63-linked polyubiquitination of RIG-I is inhibited in the presence of N protein. Our data collectively suggest that HAZV N protein interferes with the binding of TRIM25 to RIG-I and subsequent K63-linked polyubiquitination of RIG-I, which leads to inhibition of type I IFN production. Full article
(This article belongs to the Special Issue Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023)
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Review

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26 pages, 510 KiB  
Review
E3 Ubiquitin Ligases in Gammaherpesviruses and HIV: A Review of Virus Adaptation and Exploitation
by Jessica Oswald, Mathew Constantine, Adedolapo Adegbuyi, Esosa Omorogbe, Anna J. Dellomo and Elana S. Ehrlich
Viruses 2023, 15(9), 1935; https://doi.org/10.3390/v15091935 - 15 Sep 2023
Cited by 1 | Viewed by 1279
Abstract
For productive infection and replication to occur, viruses must control cellular machinery and counteract restriction factors and antiviral proteins. Viruses can accomplish this, in part, via the regulation of cellular gene expression and post-transcriptional and post-translational control. Many viruses co-opt and counteract cellular [...] Read more.
For productive infection and replication to occur, viruses must control cellular machinery and counteract restriction factors and antiviral proteins. Viruses can accomplish this, in part, via the regulation of cellular gene expression and post-transcriptional and post-translational control. Many viruses co-opt and counteract cellular processes via modulation of the host post-translational modification machinery and encoding or hijacking kinases, SUMO ligases, deubiquitinases, and ubiquitin ligases, in addition to other modifiers. In this review, we focus on three oncoviruses, Epstein–Barr virus (EBV), Kaposi’s sarcoma herpesvirus (KSHV), and human immunodeficiency virus (HIV) and their interactions with the ubiquitin–proteasome system via viral-encoded or cellular E3 ubiquitin ligase activity. Full article
(This article belongs to the Special Issue Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023)
14 pages, 2776 KiB  
Review
Pellino Proteins in Viral Immunity and Pathogenesis
by Liselotte E. Jensen
Viruses 2023, 15(7), 1422; https://doi.org/10.3390/v15071422 - 23 Jun 2023
Viewed by 1481
Abstract
Pellino proteins are a family of evolutionarily conserved ubiquitin ligases involved in intracellular signaling in a wide range of cell types. They are essential for microbe detection and the initiation of innate and adaptive immune responses. Some viruses specifically target the Pellino proteins [...] Read more.
Pellino proteins are a family of evolutionarily conserved ubiquitin ligases involved in intracellular signaling in a wide range of cell types. They are essential for microbe detection and the initiation of innate and adaptive immune responses. Some viruses specifically target the Pellino proteins as part of their immune evasion strategies. Through studies of mouse models of viral infections in the central nervous system, heart, lungs, and skin, the Pellino proteins have been linked to both beneficial and detrimental immune responses. Only in recent years have some of the involved mechanisms been identified. The objective of this review is to highlight the many diverse aspects of viral immunity and pathogenesis that the Pellino proteins have been associated with, in order to promote further research into their functions. After a brief introduction to the cellular signaling mechanisms involving Pellino proteins, their physiological roles in the initiation of immune responses, pathogenesis through excess inflammation, immune regulation, and cell death are presented. Known viral immune evasion strategies are also described. Throughout, areas that require more in-depth investigation are identified. Future research into the functions of the Pellino protein family may reveal fundamental insights into how our immune system works. Such knowledge may be leveraged in the fight against viral infections and their sequala. Full article
(This article belongs to the Special Issue Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023)
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25 pages, 2314 KiB  
Review
The Involvement of Ubiquitination and SUMOylation in Retroviruses Infection and Latency
by Taizhen Liang, Guojie Li, Yunfei Lu, Meilin Hu and Xiancai Ma
Viruses 2023, 15(4), 985; https://doi.org/10.3390/v15040985 - 17 Apr 2023
Viewed by 1766
Abstract
Retroviruses, especially the pathogenic human immunodeficiency virus type 1 (HIV-1), have severely threatened human health for decades. Retroviruses can form stable latent reservoirs via retroviral DNA integration into the host genome, and then be temporarily transcriptional silencing in infected cells, which makes retroviral [...] Read more.
Retroviruses, especially the pathogenic human immunodeficiency virus type 1 (HIV-1), have severely threatened human health for decades. Retroviruses can form stable latent reservoirs via retroviral DNA integration into the host genome, and then be temporarily transcriptional silencing in infected cells, which makes retroviral infection incurable. Although many cellular restriction factors interfere with various steps of the life cycle of retroviruses and the formation of viral latency, viruses can utilize viral proteins or hijack cellular factors to evade intracellular immunity. Many post-translational modifications play key roles in the cross-talking between the cellular and viral proteins, which has greatly determined the fate of retroviral infection. Here, we reviewed recent advances in the regulation of ubiquitination and SUMOylation in the infection and latency of retroviruses, focusing on both host defense- and virus counterattack-related ubiquitination and SUMOylation system. We also summarized the development of ubiquitination- and SUMOylation-targeted anti-retroviral drugs and discussed their therapeutic potential. Manipulating ubiquitination or SUMOylation pathways by targeted drugs could be a promising strategy to achieve a “sterilizing cure” or “functional cure” of retroviral infection. Full article
(This article belongs to the Special Issue Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023)
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20 pages, 3547 KiB  
Review
Protein Degradation by Gammaherpesvirus RTAs: More Than Just Viral Transactivators
by Lauren R. Combs, Jacob Combs, Robert McKenna and Zsolt Toth
Viruses 2023, 15(3), 730; https://doi.org/10.3390/v15030730 - 11 Mar 2023
Cited by 1 | Viewed by 2093
Abstract
Kaposi’s sarcoma-associated herpesvirus (KSHV) is a member of the Gammaherpesvirus subfamily that encodes several viral proteins with intrinsic E3 ubiquitin ligase activity or the ability to hijack host E3 ubiquitin ligases to modulate the host’s immune response and to support the viral life [...] Read more.
Kaposi’s sarcoma-associated herpesvirus (KSHV) is a member of the Gammaherpesvirus subfamily that encodes several viral proteins with intrinsic E3 ubiquitin ligase activity or the ability to hijack host E3 ubiquitin ligases to modulate the host’s immune response and to support the viral life cycle. This review focuses specifically on how the immediate-early KSHV protein RTA (replication and transcription activator) hijacks the host’s ubiquitin–proteasome pathway (UPP) to target cellular and viral factors for protein degradation to allow for robust lytic reactivation. Notably, RTA’s targets are either potent transcription repressors or they are activators of the innate and adaptive immune response, which block the lytic cycle of the virus. This review mainly focuses on what is currently known about the role of the E3 ubiquitin ligase activity of KSHV RTA in the regulation of the KSHV life cycle, but we will also discuss the potential role of other gammaherpesviral RTA homologs in UPP-mediated protein degradation. Full article
(This article belongs to the Special Issue Ubiquitin and Ubiquitin-Like Pathways in Viral Infection 2023)
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