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Multiple Roles of TRIM21 in Virus Infection
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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9867090/ https://www.ncbi.nlm.nih.gov/pubmed/36675197 http://dx.doi.org/10.3390/ijms24021683 |
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author | Li, Xue Yang, Lin Chen, Si Zheng, Jiawei Zhang, Huimin Ren, Linzhu |
author_facet | Li, Xue Yang, Lin Chen, Si Zheng, Jiawei Zhang, Huimin Ren, Linzhu |
author_sort | Li, Xue |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9867090 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98670902023-01-22 Multiple Roles of TRIM21 in Virus Infection Li, Xue Yang, Lin Chen, Si Zheng, Jiawei Zhang, Huimin Ren, Linzhu Int J Mol Sci Review 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. MDPI 2023-01-14 /pmc/articles/PMC9867090/ /pubmed/36675197 http://dx.doi.org/10.3390/ijms24021683 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Li, Xue Yang, Lin Chen, Si Zheng, Jiawei Zhang, Huimin Ren, Linzhu Multiple Roles of TRIM21 in Virus Infection |
title | Multiple Roles of TRIM21 in Virus Infection |
title_full | Multiple Roles of TRIM21 in Virus Infection |
title_fullStr | Multiple Roles of TRIM21 in Virus Infection |
title_full_unstemmed | Multiple Roles of TRIM21 in Virus Infection |
title_short | Multiple Roles of TRIM21 in Virus Infection |
title_sort | multiple roles of trim21 in virus infection |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9867090/ https://www.ncbi.nlm.nih.gov/pubmed/36675197 http://dx.doi.org/10.3390/ijms24021683 |
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