TRIM25 Identification in the Chinese Goose: Gene Structure, Tissue Expression Profiles, and Antiviral Immune Responses In Vivo and In Vitro

Wei, Yunan; Zhou, Hao; Wang, Anqi; Sun, Lipei; Wang, Mingshu; Jia, Renyong; Zhu, Dekang; Liu, Mafeng; Yang, Qiao; Wu, Ying; Sun, Kunfeng; Chen, Xiaoyue; Cheng, Anchun; Chen, Shun

doi:10.1155/2016/1403984

Cited by 10 publications

(10 citation statements)

References 46 publications

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“…The observation across species of RLR's performing compensatory mechanisms when a function or a pathway protein is absent is reiterated in birds, as MDA5 has been found to sense short and long dsRNA in chickens (372) and in the Chinese shrew (374), both of which lack RIG-I. Additionally, TRIM25 activates RIG-I in ducks (364) and in the Chinese goose (375) in the absence of the K172 activating ubiquitin binding site that is conserved in primates and some rodents (364). Finally, the rainbow trout ( Oncorhynchus mykiss ) has been found to express a LGP2 variant in addition to the canonical LGP2 that contains an incomplete C-terminal domain of RIG-I (376).…”

Section: Evolution and Speciation Of Rig-i/mda5 And Rig-i/mda5-like Pmentioning

confidence: 99%

Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5

2019

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RIG-I (Retinoic acid-inducible gene I) and MDA5 (Melanoma Differentiation-Associated protein 5), collectively known as the RIG-I-like receptors (RLRs), are key protein sensors of the pathogen-associated molecular patterns (PAMPs) in the form of viral double-stranded RNA (dsRNA) motifs to induce expression of type 1 interferons (IFN1) (IFNα and IFNβ) and other pro-inflammatory cytokines during the early stage of viral infection. While RIG-I and MDA5 share many genetic, structural and functional similarities, there is increasing evidence that they can have significantly different strategies to recognize different pathogens, PAMPs, and in different host species. This review article discusses the similarities and differences between RIG-I and MDA5 from multiple perspectives, including their structures, evolution and functional relationships with other cellular proteins, their differential mechanisms of distinguishing between host and viral dsRNAs and interactions with host and viral protein factors, and their immunogenic signaling. A comprehensive comparative analysis can help inform future studies of RIG-I and MDA5 in order to fully understand their functions in order to optimize potential therapeutic approaches targeting them.

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Section: Evolution and Speciation Of Rig-i/mda5 And Rig-i/mda5-like Pmentioning

confidence: 99%

Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5

2019

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“…The TRIM family is a large (>80 members in humans) group of E3 ubiquitin ligase proteins that share a common domain structure. Human TRIM25 is a 630 amino acid, 71 kDa E3 ubiquitin ligase that is widely expressed across human cell types and is conserved among vertebrates including fish, birds and mammals (Fagerberg et al, 2014;Feng et al, 2015;Orimo, Inoue, Ikeda, Noji, & Muramatsu, 1995;Wei et al, 2016;Yang et al, 2016). Like other TRIM family proteins, it consists of an N-terminal zinc-finger Really Interesting New Gene (RING) domain, responsible for its E3 ubiquitin ligase activity, two B-box zinc finger domains of unknown function, a coiled-coil domain (CCD), responsible for homo and heterodimerization, with a linker domain leading to a C-terminal associated with SPRY/SPla and the RYanodine receptor (PRY/SPRY) domain, responsible for protein-protein interactions.…”

Section: Trim25 Is An E3 Ubiquitin Ligasementioning

confidence: 99%

TRIM25 and its emerging RNA‐binding roles in antiviral defense

2020

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The innate immune system is the body's first line of defense against viruses, with pattern recognition receptors (PRRs) recognizing molecules unique to viruses and triggering the expression of interferons and other anti-viral cytokines, leading to the formation of an anti-viral state. The tripartite motif containing 25 (TRIM25) is an E3 ubiquitin ligase thought to be a key component in the activation of signaling by the PRR retinoic acid-inducible gene I protein (RIG-I). TRIM25 has recently been identified as an RNA-binding protein, raising the question of whether its RNA-binding activity is important for its role in innate immunity. Here, we review TRIM25's mechanisms and pathways in noninfected and infected cells. We also introduce models that explain how

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“…The nonstructural protein 1 (NS1) of influenza A and B virus (IAV/IBV) has been characterized as a viral antagonist of host innate immunity through interactions with TRIM25 [ 57 , 100 , 240 , 241 ]. As described above, TRIM25 plays a critical role in the activation of the RLR pathways [ 57 , 242 , 243 ]. The NS1 protein from IAV directly interacts with the coiled-coil domain of TRIM25 to impede its multimerization [ 57 , 244 ].…”

Section: Viral Antagonism Of Trimsmentioning

confidence: 99%

The TRIMendous Role of TRIMs in Virus–Host Interactions

et al. 2017

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The innate antiviral response is integral in protecting the host against virus infection. Many proteins regulate these signaling pathways including ubiquitin enzymes. The ubiquitin-activating (E1), -conjugating (E2), and -ligating (E3) enzymes work together to link ubiquitin, a small protein, onto other ubiquitin molecules or target proteins to mediate various effector functions. The tripartite motif (TRIM) protein family is a group of E3 ligases implicated in the regulation of a variety of cellular functions including cell cycle progression, autophagy, and innate immunity. Many antiviral signaling pathways, including type-I interferon and NF-κB, are TRIM-regulated, thus influencing the course of infection. Additionally, several TRIMs directly restrict viral replication either through proteasome-mediated degradation of viral proteins or by interfering with different steps of the viral replication cycle. In addition, new studies suggest that TRIMs can exert their effector functions via the synthesis of unconventional polyubiquitin chains, including unanchored (non-covalently attached) polyubiquitin chains. TRIM-conferred viral inhibition has selected for viruses that encode direct and indirect TRIM antagonists. Furthermore, new evidence suggests that the same antagonists encoded by viruses may hijack TRIM proteins to directly promote virus replication. Here, we describe numerous virus–TRIM interactions and novel roles of TRIMs during virus infections.

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TRIM25 Identification in the Chinese Goose: Gene Structure, Tissue Expression Profiles, and Antiviral Immune Responses In Vivo and In Vitro

Cited by 10 publications

References 46 publications

Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5

Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5

TRIM25 and its emerging RNA‐binding roles in antiviral defense

The TRIMendous Role of TRIMs in Virus–Host Interactions

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