TRIM21 inhibits porcine epidemic diarrhea virus proliferation by proteasomal degradation of the nucleocapsid protein

Wang, Hua; Chen, Xiaoyong; Kong, Ning; Jiao, Yajuan; Sun, Dage; Dong, Sujie; Qin, Wenzhen; Zhai, Huanjie; Yu, Lingxue; Zheng, Hao; Wu, Tong; Yu, Hai; Tong, Guangzhi; Shan, Tongling

doi:10.1007/s00705-021-05080-4

Cited by 20 publications

(21 citation statements)

References 30 publications

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“…Interestingly, most of the target proteins are involved in proteasome, ribosome, spliceosome, Epstein-Barr virus infection, RNA degradation, and the carbon metabolism pathway. The proteasome pathway is closely related to virus infection, for example, an active ubiquitin proteasome system is necessary for efficient replication of infectious bronchitis virus in Vero cells [ 35 , 36 ]. TRIM21 inhibits porcine epidemic diarrhea virus proliferation by proteasomal degradation of the nucleocapsid protein [ 36 ].…”

Section: Resultsmentioning

confidence: 99%

“…The proteasome pathway is closely related to virus infection, for example, an active ubiquitin proteasome system is necessary for efficient replication of infectious bronchitis virus in Vero cells [ 35 , 36 ]. TRIM21 inhibits porcine epidemic diarrhea virus proliferation by proteasomal degradation of the nucleocapsid protein [ 36 ]. Also, SARS-CoV-2 hijacks folate and one-carbon metabolism for viral replication [ 37 ].…”

Section: Resultsmentioning

confidence: 99%

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Construction, Identification and Analysis of the Interaction Network of African Swine Fever Virus MGF360-9L with Host Proteins

Yang

Zhang

Shi

et al. 2021

Viruses

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African swine fever virus (ASFV) is prevalent in many countries and is a contagious and lethal virus that infects pigs, posing a threat to the global pig industry and public health. The interaction between the virus and the host is key to unlocking the mystery behind viral pathogenesis. A comprehensive understanding of the viral and host protein interaction may provide clues for developing new antiviral strategies. Here, we show a network of ASFV MGF360-9L protein interactions in porcine kidney (PK-15) cells. Overall, 268 proteins that interact with MGF360-9L are identified using immunoprecipitation and liquid chromatography–mass spectrometry (LC-MS). Accordingly, gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses were conducted, and the protein–protein interaction (PPI) network was created. It was speculated that the cellular proteins interacting with MGF360-9L are involved in protein binding, metabolism, and the innate immune response. Proteasome subunit alpha type (PSMA3), 26S protease regulatory subunit 4 (PSMC1), autophagy and beclin 1 regulator 1 (AMBRA1), and DEAD-box helicase 20 (DDX20) could interact with MGF360-9L in vitro. PSMA3 and PSMC1 overexpression significantly promoted ASFV replication, and MGF360-9L maintained the transcriptional level of PSMA3 and PSMC1. Here, we show the interaction between ASFV MGF360-9L and cellular proteins and elucidate the virus–host interaction network, which effectively provides useful protein-related information that can enable further study of the potential mechanism and pathogenesis of ASFV infection.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Construction, Identification and Analysis of the Interaction Network of African Swine Fever Virus MGF360-9L with Host Proteins

Yang

Zhang

Shi

et al. 2021

Viruses

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“…Additionally, Porcine Epidemic Diarrhoea Virus (PEDV) is inhibited by TRIM21, which targets the nucleoprotein for proteasomal degradation. Conversely, following in vitro PEDV infection, the endogenous expression of TRIM21 was downregulated, increasing both PEDV viral titres and nucleoprotein levels (98).…”

Section: Other Interactionsmentioning

confidence: 99%

TRIM21/Ro52 - Roles in Innate Immunity and Autoimmune Disease

2021

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TRIM21 (Ro52/SSA1) is an E3 ubiquitin ligase with key roles in immune host defence, signal transduction, and possibly cell cycle regulation. It is also an autoantibody target in Sjögren’s syndrome, systemic lupus erythematosus, and other rheumatic autoimmune diseases. Here, we summarise the structure and function of this enzyme, its roles in innate immunity, adaptive immunity and cellular homeostasis, the pathogenesis of autoimmunity against TRIM21, and the potential impacts of autoantibodies to this intracellular protein.

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“…TRIM21 catalyzes the formation of Lys63 (K63)-linked ubiquitin chains and activates the NF-κB, AP-1, and IRF signaling pathways ( McEwan et al, 2013 ). However, in porcine epidemic diarrhea virus (PEDV) infection, TRIM21 exhibits a different strategy; TRIM21 was found to interact and colocalize with the N protein, inducing the degradation of the N protein in a proteasome-dependent manner ( Wang et al, 2021 ).…”

Section: Viral Utilization Of Trimsmentioning

confidence: 99%

“…There is evidence to show that the coronaviral nucleocapsid (N) protein suppresses TRIM25 activity to defend against human immune response ( Hu et al, 2017 ; Chang et al, 2020 ; Oh and Shin, 2021 ). On the other hand, the N protein can be degraded by TRIM21 ( Wang et al, 2021 ). It is therefore of urgent interest to clarify the dynamic interaction of the N protein with TRIMs, which can provide new clues to understand coronavirus pathogenesis.…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Regulation of Tripartite Motif-Containing Proteins on Immune Response and Viral Evasion

Zhang

Wang

2021

Front. Microbiol.

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Tripartite motif-containing proteins (TRIMs), exhibiting ubiquitin E3 ligase activity, are involved in regulation of not only autophagy and apoptosis but also pyrotosis and antiviral immune responses of host cells. TRIMs play important roles in modulating signaling pathways of antiviral immune responses via type I interferon, NF-κB, Janus kinase/signal transducer and activator of transcription (JAK/STAT), and Nrf2. However, viruses are able to antagonize TRIM activity or evenly utilize TRIMs for viral replication. This communication presents the current understanding of TRIMs exploited by viruses to evade host immune response.

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TRIM21 inhibits porcine epidemic diarrhea virus proliferation by proteasomal degradation of the nucleocapsid protein

Cited by 20 publications

References 30 publications

Construction, Identification and Analysis of the Interaction Network of African Swine Fever Virus MGF360-9L with Host Proteins

Construction, Identification and Analysis of the Interaction Network of African Swine Fever Virus MGF360-9L with Host Proteins

TRIM21/Ro52 - Roles in Innate Immunity and Autoimmune Disease

Regulation of Tripartite Motif-Containing Proteins on Immune Response and Viral Evasion

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