RING-Domain E3 Ligase-Mediated Host–Virus Interactions: Orchestrating Immune Responses by the Host and Antagonizing Immune Defense by Viruses
Open accessAbstract
The RING-domain E3 ligases (RING E3s), a group of E3 ligases containing one or two RING finger domains, are involved in various cellular processes such as cell proliferation, immune regulation, apoptosis, among others. In the host, a substantial number of the RING E3s have been implicated to inhibit viral replication through regulating immune responses, including activation and inhibition of retinoic acid-inducible gene I-like receptors, toll-like receptors, and DNA receptor signaling pathways, modulation of cell-surface expression of major histocompatibility complex, and co-stimulatory molecules. During the course of evolution and adaptation, viruses encode RING E3s to antagonize host immune defense, such as the infected cell protein 0 of herpes simplex virus type 1, the non-structural protein 1 of rotavirus, and the K3 and K5 of Kaposi's sarcoma-associated herpesvirus. In addition, recent studies suggest that viruses can hijack the host RING E3s to facilitate viral replication. Based on emerging and interesting discoveries, the RING E3s present novel links among the host and viruses. Herein, we focus on the latest research progresses in the RING E3s-mediated host-virus interactions and discuss the outlooks of the RING E3s for future research.
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Viral proteins bind and redirect specific E3 ligases to ubiquitinate certain host proteins and enhance viral replication.
“Viral proteins bind and thereby redirect specific E3 ligases to ubiquitinate certain host proteins and enhance viral replication.”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [91]
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Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works
- Authors
- Zhang, Y., Li, L.-F., Munir, M., & Qiu, H.-J.
- Affiliations
- Chinese Academy of Agricultural Sciences (CN)
- Lancaster University (GB)
- Corresponding author
- Qiu, Hua-Ji
- Venue
- Frontiers in Immunology
- Publisher
- Frontiers Media SA
- Published
- 2018-05-22
- Volume
- 9
- Pages
- 1083-1083
- ISSN
- 1664-3224 (ISSN-L)
- PMC
- PMC5972323
- OpenAlex
- W2804263829
- Cited by
- 62
- References
- 132
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 7 · 2023: 4 · 2022: 11 · 2021: 9 · 2020: 5 · 2019: 12 · 2018: 2
- FWCI
- 0.72
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Frontiers in Immunology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Lancaster EPrints (Lancaster University) (submittedVersion)
- Funders
- National Natural Science Foundation of China (31630080, 31702220, and 31572540)
- Natural Science Foundation of Heilongjiang Province (QC2017027)
- China Postdoctoral Science Foundation (2017M620979)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- host-virus interaction, viral immune evasion, antiviral immunity, RIG-I-like receptors, Toll-like receptors, MHC class I expression, costimulatory molecules, viral replication, ubiquitination
- MeSH terms
- Animals, Humans, Immunity, Protein Binding, Structure-Activity Relationship, Viral Proteins, Virus Diseases, Viruses, Signal Transduction, Biomarkers, Ubiquitin-Protein Ligases, Protein Interaction Domains and Motifs, Host-Pathogen Interactions, Immunomodulation
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