期刊
VIRUS RESEARCH
卷 311, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.virusres.2022.198690
关键词
Tripartite motif 26 (TRIM26); Porcine reproductive and respiratory syndrome; virus (PRRSV); Nucleocapsid (N) protein; Virus-host interactions; Replication
类别
资金
- National Natural Sciences Foun-dation of China [32002265]
- Natural Science Foundation of Henan Province [202300410187]
- Key Technologies Research and Devel-opment Program of Henan Province [202102110095, 202102110247]
- Scientific Research Innovation Team of Veterinary Bio-technology [2018KYTD16]
TRIM26 can potentially be a target for drug design against PRRSV as it can inhibit virus replication and induce degradation of the N protein. Depletion of TRIM26 leads to increased viral RNA and virus yield. The antiviral activity of TRIM26 is dependent on specific domains.
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.
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