TRIM21 restricts influenza A virus replication by ubiquitination-dependent degradation of M1
文献类型: 外文期刊
第一作者: Lin, Lulu
作者: Lin, Lulu;Wang, Xingbo;Deng, Tingjuan;Yan, Yan;Dong, Weiren;Zhou, Jiyong;Lin, Lulu;Zhou, Jiyong;Chen, Zhen;Huang, Yu
作者机构:
期刊名称:PLOS PATHOGENS ( 影响因子:6.7; 五年影响因子:6.7 )
ISSN: 1553-7366
年卷期: 2023 年 19 卷 6 期
页码:
收录情况: SCI
摘要: Author summaryIAVs use various adaptive mutation strategies to evade host restriction. In the present study, we found that TRIM21 in mammals directly bound to M1 R-95 site resulted in proteasome-degradation of M1 via K48-linked ubiquitination at K-242 and thereby inhibited replication of IAV, which caused inhibitory pressure for host adaptive mutation of IAVs at R-95 of M1. This study highlights the association between host restriction factor and virus evolution. Tripartite motif-containing protein 21 (TRIM21), an E3 ubiquitin ligase, plays a critical role in the host antiviral response. However, the mechanism and antiviral spectrum of TRIM21 in influenza A virus (IAV) remain unclear. Here, we report that TRIM21 inhibits the replication of various IAV subtypes by targeting matrix protein 1 (M1) from H3/H5/H9, but not H1 and H7 M1. Mechanistically, TRIM21 binds to the residue R-95 of M1 and facilitates K48 ubiquitination of M1 K242 for proteasome-dependent degradation, leading to the inhibition of H3, H5, and H9 IAV replication. Interestingly, the recombinant viruses with M1 (RK)-K-95 or (KR)-R-242 mutations were resistance to TRIM21 and exhibited more robust replication and severe pathogenicity. Moreover, the amino acid sequence M1 proteins, mainly from avian influenza such as H5N1, H7N9, H9N2, ranging from 1918 to 2022, reveals a gradual dominant accumulation of the TRIM21-driven (RK)-K-95 mutation when the virus jumps into mammals. Thus, TRIM21 in mammals' functions as a host restriction factor and drives a host adaptive mutation of influenza A virus.
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