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Avian Metapneumovirus Subgroup C Induces Mitochondrial Antiviral Signaling Protein Degradation through the Ubiquitin-Proteasome Pathway

文献类型： 外文期刊

作者： Hou, Lei 1 ; Hu, Xiaohan 4 ; Guo, Jinshuo 2 ; Quan, Rong 1 ; Wei, Li 1 ; Wang, Jing 1 ; Song, Jiangwei 1 ; Liu, Jue 1 ;

作者机构： 1.Beijing Acad Agr & Forestry Sci, Beijing Key Lab Prevent & Control Infect Dis Live, Inst Anim Husb & Vet Med, Beijing 100097, Peoples R China

2.Yangzhou Univ, Coll Vet Med, Yangzhou 225009, Jiangsu, Peoples R China

3.Yangzhou Univ, Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou 225009, Jiangsu, Peoples R China

4.Fujian Agr & Forestry Univ, Coll Anim Sci, Coll Bee Sci, Fuzhou 350002, Peoples R China

关键词： MAVS; ubiquitination; degradation; E3 ubiquitin ligase; aMPV/C

期刊名称：VIRUSES-BASEL （ 影响因子：5.048； 五年影响因子：5.127 ）

ISSN：

年卷期： 2021 年 13 卷 10 期

页码：

收录情况： SCI

摘要： The mitochondrial antiviral signaling (MAVS) protein, a critical adapter, links the upstream recognition of viral RNA to downstream antiviral signal transduction. However, the interaction mechanism between avian metapneumovirus subgroup C (aMPV/C) infection and MAVS remains unclear. Here, we confirmed that aMPV/C infection induced a reduction in MAVS expression in Vero cells in a dose-dependent manner, and active aMPV/C replication was required for MAVS decrease. We also found that the reduction in MAVS occurred at the post-translational level rather than at the transcriptional level. Different inhibitors were used to examine the effect of proteasome or autophagy on the regulation of MAVS. Treatment with a proteasome inhibitor MG132 effectively blocked MAVS degradation. Moreover, we demonstrated that MAVS mainly underwent K48-linked ubiquitination in the presence of MG132 in aMPV/C-infected cells, with amino acids 363, 462, and 501 of MAVS being pivotal sites in the formation of polyubiquitin chains. Finally, E3 ubiquitin ligases for MAVS degradation were screened and identified and RNF5 targeting MAVS at Lysine 363 and 462 was shown to involve in MAVS degradation in aMPV/C-infected Vero cells. Overall, these results reveal the molecular mechanism underlying aMPV/C infection-induced MAVS degradation by the ubiquitin-proteasome pathway.

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