Abstract
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.
Highlights
In vertebrates, the immune system is composed of the innate and adaptive components
The RING E3s are divided into five subfamilies, each of which has its own special functions
The RING-Ub interacting motif (UIM) family is related to T cell activation, the membrane-associated RING-CH (MARCH) family has been identified to inhibit antigen presentation through degrading cellular receptors and costimulatory molecules, and the tripartite motif-containing (TRIM) family restricts virus replication through direct interactions with viral proteins
Summary
The immune system is composed of the innate and adaptive components. The innate immune system is a highly effective first-line of defense to detect and fight against invading pathogens, and it is initiated when pattern recognition receptors (PRRs) recognize pathogenassociated molecular patterns (PAMPs) [1, 2]. Cumulative actions of both innate and adaptive immune systems provide powerful defense against pathogens To accomplish such enormous and elaborative defense tasks, the immune system is under strict and precise regulation. The RING E3s positively regulate immune system to amplify the antiviral responses and negatively regulate immune system to decrease the magnitude and duration of immune responses for appropriate antiviral immunity These counter-actions of the RING E3s indicate that they orchestrate immune responses at the interface of host–virus interactions. Recent studies suggest that viruses hijack the host RING E3s to promote viral replication through antagonizing IFN-mediated antiviral responses and ubiquitination of viral proteins. We review the mechanisms of the host RING E3s in regulating immune responses and the functions of the RING E3s encoded or hijacked by viruses in viral replication
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