Multiple Roles of TRIM21 in Virus Infection

Int J Mol Sci. 2023 Jan 14;24(2):1683. doi: 10.3390/ijms24021683.

Abstract

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.

Keywords: interaction; tripartite motif protein 21 (TRIM21); viruses.

Publication types

  • Review

MeSH terms

  • Cytosol / metabolism
  • Humans
  • Proteins / metabolism
  • Ribonucleoproteins* / genetics
  • Ribonucleoproteins* / metabolism
  • Tripartite Motif Proteins / genetics
  • Tripartite Motif Proteins / metabolism
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitination
  • Virus Diseases* / genetics
  • Virus Diseases* / metabolism

Substances

  • Proteins
  • Tripartite Motif Proteins
  • Ubiquitin-Protein Ligases
  • SS-A antigen
  • Ribonucleoproteins