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• W3157385474 abstract "TRIM33 is a member of the tripartite motif (TRIM) superfamily which contributes to regulate a multitude of cellular processes, including innate immune responses. Viperin_sv1 has recently been identified as a novel splice variant of viperin that triggers a strong antiviral effect by activating the interferon signaling pathway. SVCV infection is known to cause the degradation of viperin_sv1 through a proteasome pathway; however, the underlying mechanism remains unsolved. In this study, we identify that TRIM33 protein interacts and colocalizes with viperin_sv1 protein to induce its degradation. Additional analysis revealed that the N-terminus, but not the C-terminus, region of TRIM33 is essential for interacting with and inducing the degradation of viperin_sv1 protein. Moreover, SVCV infection enhances the expression of TRIM33 which is proved to reduce the type-1 interferon response and to promote viral replication. In conclusion, our study demonstrates that TRIM33 enhances the replication of SVCV by dampening the antiviral protein viperin_sv1 expression. These findings may lay a foundation for developing novel therapeutic strategies to halt SVCV infection. • TRIM33 was identified as the E3 ligase interacting with and degrading the viperin_sv1 protein. • The mRNA expression level of TRIM33 is increased upon SVCV infection. • The N-terminus region of TRIM33 associates with the viperin_sv1 degradation. • The overexpression of TRIM33 could promote the replication of SVCV by reducing the IFN production." @default.
• W3157385474 created "2021-05-10" @default.
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• W3157385474 date "2021-09-01" @default.
• W3157385474 modified "2023-10-16" @default.
• W3157385474 title "TRIM33 promotes spring viremia of carp virus replication by degrading the antiviral protein viperin_sv1" @default.
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• W3157385474 doi "https://doi.org/10.1016/j.aquaculture.2021.736837" @default.
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