Multiple Roles of TRIM21 in Virus Infection

被引:13
作者
Li, Xue [1 ]
Yang, Lin [1 ]
Chen, Si [1 ]
Zheng, Jiawei [1 ]
Zhang, Huimin [1 ]
Ren, Linzhu [1 ]
机构
[1] Jilin Univ, Coll Anim Sci, Key Lab Zoonoses Res, Minist Educ, 5333 Xian Rd, Changchun 130062, Peoples R China
基金
中国国家自然科学基金;
关键词
tripartite motif protein 21 (TRIM21); viruses; interaction; NEGATIVE REGULATION; EMERGING ROLES; FC-RECEPTOR; NEUTRALIZATION; IMMUNITY; PROTEIN; UBIQUITINATION; DEGRADATION; ACTIVATION;
D O I
10.3390/ijms24021683
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The tripartite motif protein 21 (TRIM21) belongs to the TRIM family, possessing an E3 ubiquitin ligase activity. Similar to other TRIMs, TRIM21 also contains three domains (named RBCC), including the Really Interesting New Gene (RING) domain, one or two B-Box domains (B-Box), and one PRY/SPRY domain. Notably, we found that the RING and B-Box domains are relatively more conservative than the PRY/SPRY domain, suggesting that TRIM21 of different species had similar functions. Recent results showed that TRIM21 participates in virus infection by directly interacting with viral proteins or modulating immune and inflammatory responses. TRIM21 also acts as a cytosol high-affinity antibody Fc receptor, binding to the antibody-virus complex and triggering an indirect antiviral antibody-dependent intracellular neutralization (ADIN). This paper focuses on the recent progress in the mechanism of TRIM21 during virus infection and the application prospects of TRIM21 on virus infection.
引用
收藏
页数:16
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