TRIM59 inhibits porcine reproductive and respiratory syndrome virus (PRRSV)-2 replication in vitro

Jing, Huiyuan; Ke, Wenting; Tao, Ran; Li, Yang; Zhao, Yabo; Cao, Sufang; Sun, Yuhua; Wang, Jinhe; Zhang, Yan; Wang, Dong; Zhao, Pandeng; Duan, Erzhen

doi:10.1016/j.rvsc.2019.10.004

Cited by 11 publications

(9 citation statements)

References 64 publications

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“…Additional recent studies identifying inhibition of viral proteins by TRIMs included TRIM28 and TRIM59. TRIM28, a nuclear protein that is known to have transcriptional regulatory activity [ 57 ] and is a known repressor of endogenous retroviruses [ 58 ], has been recently reported to restrict viral integration of HIV-1 by binding and inhibiting the active, acetylated form of the viral integrase host [ 29 , 59 ], while TRIM59 interacts with the porcine reproductive and respiratory syndrome virus (PRRSV) nsp11 to inhibit infection [ 60 ]. Finally, TRIM69 inhibits viral transcription and the formation of VSV replication compartments, reducing the synthesis of viral RNA and, therefore, the inhibition of viral replication [ 61 ].…”

Section: Antiviral Activity Of Trim Proteinsmentioning

confidence: 99%

TRIM Proteins in Host Defense and Viral Pathogenesis

Giraldo

Hage

Tol

et al. 2020

Curr Clin Micro Rpt

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Purpose of Review Tripartite motif (TRIM) proteins are a large group of E3 ubiquitin ligases involved in different cellular functions. Of special interest are their roles in innate immunity, inflammation, and virus replication. We discuss novel roles of TRIM proteins during virus infections that lead to increased pathogenicity. Recent Findings TRIM proteins regulate different antiviral and inflammatory signaling pathways, mostly by promoting ubiquitination of important factors including pattern recognition receptors, adaptor proteins, kinases, and transcription factors that are involved in type I interferon and NF-κB pathways. Therefore, viruses have developed mechanisms to target TRIMs for immune evasion. New evidence is emerging indicating that viruses have the ability to directly use TRIMs and the ubiquitination process to enhance the viral replication cycle and cause increased pathogenesis. A new report on TRIM7 also highlights the potential pro-viral role of TRIMs via ubiquitination of viral proteins and suggests a novel mechanism by which ubiquitination of virus envelope protein may provide determinants of tissue and species tropism. Summary TRIM proteins have important functions in promoting host defense against virus infection; however, viruses have adapted to evade TRIM-mediated immune responses and can hijack TRIMs to ultimately increase virus pathogenesis. Only by understanding specific TRIM-virus interactions and by using more in vivo approaches can we learn how to harness TRIM function to develop therapeutic approaches to reduce virus pathogenesis.

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Section: Antiviral Activity Of Trim Proteinsmentioning

confidence: 99%

TRIM Proteins in Host Defense and Viral Pathogenesis

Giraldo

Hage

Tol

et al. 2020

Curr Clin Micro Rpt

View full text Add to dashboard Cite

show abstract

“…TRIM21 [ 29 ], TRIM22 [ 30 ], TRIM25 [ 31 ] and TRIM59 [ 32 ] have been reported to inhibit PRRSV replication, but the mechanism is unknown. TRIM22 and TRIM25 do not ubiquitinate and degrade PRRSV N protein, and N protein impairs TRIM25-mediated RIG-I ubiquitination to suppress interferon-beta production.…”

Section: Discussionmentioning

confidence: 99%

TRIM4-mediated ubiquitination of NSP2 restricts porcine reproductive and respiratory syndrome virus proliferation

et al. 2022

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Porcine reproductive and respiratory syndrome (PRRS) is a highly contagious and virulent infectious disease caused by the porcine reproductive and respiratory syndrome virus (PRRSV), which has substantial economic losses in the pig industry worldwide, and PRRSV attenuated vaccines and inactivated vaccines do have limitations in immune protection. The discovery of new antiviral targets has become a new research field. The proteomic studies have shown that the PRRSV NSP2 protein interacts with tripartite motif protein 4 (TRIM4), but it was still unknown whether TRIM4 regulates PRRSV infections. In this study, the TRIM4 gene from Marc-145 cells was cloned, and it was proved that TRIM4 overexpression inhibits PRRSV replication, whereas TRIM4 small-interfering-RNA knockdown resulted in increased virus titers. Mechanism investigation indicated that TRIM4 inhibits PRRSV replication through ubiquitination and degradation of the NSP2 protein. Protease inhibitor MG132 (carbobenzoxy-Leu-Leu-leucinal) attenuated the TRIM4-driven degradation of NSP2. Taken together, TRIM4 impairs PRRSV proliferation via ubiquitination and degradation of NSP2.

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“…TRIM proteins are key components of the innate immune system as a new class of host antiviral restriction factors (Hatakeyama, 2017). TRIM59 has been identified as a potential nsp11-binding partner to inhibit PRRSV replication in vitro (Jing et al, 2019a). TRIM25 also inhibits PRRSV replication whereas the N protein antagonizes the antiviral activity by interfering with TRIM25-mediated RIG-I ubiquitination (Zhao et al, 2019).…”

Section: Other Cellular Pathways Involved In Prrsv Proliferationmentioning

confidence: 99%

Molecular and Cellular Mechanisms for PRRSV Pathogenesis and Host Response to Infection

et al. 2020

Virus Research

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TRIM59 inhibits porcine reproductive and respiratory syndrome virus (PRRSV)-2 replication in vitro

Cited by 11 publications

References 64 publications

TRIM Proteins in Host Defense and Viral Pathogenesis

TRIM Proteins in Host Defense and Viral Pathogenesis

TRIM4-mediated ubiquitination of NSP2 restricts porcine reproductive and respiratory syndrome virus proliferation

Molecular and Cellular Mechanisms for PRRSV Pathogenesis and Host Response to Infection

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