Characterization of porcine tripartite motif genes as host restriction factors against PRRSV and PEDV infection

Wei, Ying; Zou, Chuangchao; Zeng, Sha; Xue, Chunyi; Cao, Yongchang

doi:10.1016/j.virusres.2019.197647

Cited by 13 publications

(8 citation statements)

References 45 publications

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“…There is a variation in the number of TRIM genes expressed by different species. TRIM25 is one of several TRIM members that are activated in both human and pig cells in response to IFN treatment, and the transcription of porcine TRIM25 is increased in PAMs infected with RNA viruses of concern (Wei et al, 2019), indicating porcine TRIM25 as an important host factor. We first identified porcine TRIM25's roles on the NLRP3 inflammasome-mediated IL-1β production by utilizing the previously set-up porcine NLRP3 inflammasome reconstitution system (Park et al, 2018).…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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NLRP3 Inflammasome Activation Enhanced by TRIM25 is Targeted by the NS1 Protein of 2009 Pandemic Influenza A Virus

Park

Pandey

et al. 2021

Front. Microbiol.

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Nucleotide-binding domain and leucine-rich repeat-containing protein 3 (NLRP3) inflammasome-mediated interleukin-1 beta (IL-1β) production is one of the crucial responses in innate immunity upon infection with viruses including influenza A virus (IAV) and is modulated by both viral and host cellular proteins. Among host proteins involved, we identified tripartite motif-containing protein 25 (TRIM25) as a positive regulator of porcine NLRP3 inflammasome-mediated IL-1β production. TRIM25 achieved this function by enhancing the pro-caspase-1 interaction with apoptosis-associated speck-like protein containing caspase recruitment domain (ASC). The N-terminal RING domain, particularly residues predicted to be critical for the E3 ligase activity of TRIM25, was responsible for this enhancement. However, non-structural protein 1 (NS1) C-terminus of 2009 pandemic IAV interfered with this action by interacting with TRIM25, leading to diminished association between pro-caspase-1 and ASC. These findings demonstrate that TRIM25 promotes the IL-1β signaling, while it is repressed by IAV NS1 protein, revealing additional antagonism of the NS1 against host pro-inflammatory responses.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

NLRP3 Inflammasome Activation Enhanced by TRIM25 is Targeted by the NS1 Protein of 2009 Pandemic Influenza A Virus

Park

Pandey

et al. 2021

Front. Microbiol.

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“…Notably, PEDV infection downregulates endogenous expression of TRIM21 in African green monkey kidney cells (Vero cells) and porcine kidney cells (LLC-PK1 cells) [ 26 ]. However, another group reported that the expression of TRIM21 was upregulated after PEDV infection in porcine alveolar macrophages [ 27 ]. Therefore, the reason for the significant difference of TRIM21 expression in different cells during PEDV infection needs to be further clarified.…”

Section: Potential Mechanisms Of Trim21 In Virus Infectionmentioning

confidence: 99%

Multiple Roles of TRIM21 in Virus Infection

Yang

Chen

et al. 2023

IJMS

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The tripartite motif protein 21 (TRIM21) belongs to the TRIM family, possessing an E3 ubiquitin ligase activity. Similar to other TRIMs, TRIM21 also contains three domains (named RBCC), including the Really Interesting New Gene (RING) domain, one or two B-Box domains (B-Box), and one PRY/SPRY domain. Notably, we found that the RING and B-Box domains are relatively more conservative than the PRY/SPRY domain, suggesting that TRIM21 of different species had similar functions. Recent results showed that TRIM21 participates in virus infection by directly interacting with viral proteins or modulating immune and inflammatory responses. TRIM21 also acts as a cytosol high-affinity antibody Fc receptor, binding to the antibody–virus complex and triggering an indirect antiviral antibody-dependent intracellular neutralization (ADIN). This paper focuses on the recent progress in the mechanism of TRIM21 during virus infection and the application prospects of TRIM21 on virus infection.

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“…Tripartite motif-containing 72 (TRIM72), also known as Mitsugumin-53 (MG53), is an E3 ubiquitin ligase that belongs to the TRIM family [8], which is involved in various pathological processes, including immunity, infection, and cancer [9,10]. Originally, TRIM72 deficiency was associated with various tissue injuries, including muscular dystrophy, heart failure, lung injury, and kidney disease [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

TRIM72 exerts antitumor effects in breast cancer and modulates lactate production and MCT4 promoter activity by interacting with PPP3CA

Wang

et al. 2022

Anti-Cancer Drugs

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A hypoxic tumor microenvironment (TME) promotes cancer progression, yet its value as a therapeutic target remains underexploited. Tripartite motif-containing 72 (TRIM72) may protect cells against various stresses including hypoxia. Recently, low TRIM72 expression has been implicated in cancer progression. However, the biological role and molecular mechanism of TRIM72 in breast cancer (BC) remain unclear. Herein, we analyzed the TRIM72 expression in BC tissue and cell lines by western blot (WB) and quantitative reverse transcription-PCR. We established the overexpression of TRIM72 using plasmids and lentiviral-mediated upregulation, as well as downregulation of protein phosphatase 3 catalytic subunit alpha (PPP3CA) by siRNA. The tumor-suppressive roles of TRIM72 were assessed on BT549 and MDA-MB-231 cells by MTS, Transwell, and flow cytometry assays in vitro and in xenografted tumors in vivo . The molecular mechanism of TRIM72 was investigated by luciferase reporter and co-immunoprecipitation (Co-IP) assay. Lactate production was measured by ELISA under hypoxic environments induced by CoCl 2 . Moreover, the expression of PI3K/Akt/mTOR pathway-associated proteins was detected by WB in BC cells. Results showed that TRIM72 was downregulated in BC. Overexpression of TRIM72 inhibited tumor proliferation and invasion in vitro and in a xenograft tumor model. Mechanistically, PPP3CA altered the inhibitory effects of TRIM72 on hypoxia-induced lactate production and monocarboxylate transporter 4-promoter activity, as well as the effect of the PI3K/Akt/mTOR signaling pathway. Our study suggests that TRIM72 modulates the TME and plays tumor-suppressive roles in BC progression. Therefore, TRIM72 may serve as a potential therapeutic target in BC.

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Characterization of porcine tripartite motif genes as host restriction factors against PRRSV and PEDV infection

Cited by 13 publications

References 45 publications

NLRP3 Inflammasome Activation Enhanced by TRIM25 is Targeted by the NS1 Protein of 2009 Pandemic Influenza A Virus

NLRP3 Inflammasome Activation Enhanced by TRIM25 is Targeted by the NS1 Protein of 2009 Pandemic Influenza A Virus

Multiple Roles of TRIM21 in Virus Infection

TRIM72 exerts antitumor effects in breast cancer and modulates lactate production and MCT4 promoter activity by interacting with PPP3CA

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