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- W4207023265 endingPage "198690" @default.
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- W4207023265 abstract "Porcine reproductive and respiratory syndrome (PRRS), caused by PRRSV, has ranked among the most economically important veterinary infectious diseases globally. Recently, tripartite motif (TRIMs) family members have arisen as novel restriction factors in antiviral immunity. Noteworthy, TRIM26 was reported as a binding partner of IRF3, TBK1, TAB1, and NEMO, yet its role in virus infection remains controversial. Herein, we showed that TRIM26 bound N protein by the C-terminal PRY/SPRY domain. Moreover, ectopic expression of TRIM26 impaired PRRSV replication and induced degradation of N protein. The anti-PRRSV activity was independent of the nuclear localization signal (NLS). Instead, deletion of the RING domain, or the PRY/SPRY portion, abrogated the antiviral function. Finally, siRNA depletion of TRIM26 resulted in enhanced production of viral RNA and virus yield in porcine alveolar macrophages (PAMs) after PRRSV infection. Overexpression of an RNAi-resistant TRIM26 rescue-plasmid led to the acquisition of PRRSV restriction in TRIM26-knockdown cells. Together, these data add TRIM26 as a potential target for drug design against PRRSV." @default.
- W4207023265 created "2022-01-26" @default.
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- W4207023265 date "2022-04-01" @default.
- W4207023265 modified "2023-09-29" @default.
- W4207023265 title "TRIM26-mediated degradation of nucleocapsid protein limits porcine reproductive and respiratory syndrome virus-2 infection" @default.
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- W4207023265 doi "https://doi.org/10.1016/j.virusres.2022.198690" @default.
- W4207023265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35077707" @default.
- W4207023265 hasPublicationYear "2022" @default.
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