Interplay between TRIM7 and antiviral immunity

Front Cell Infect Microbiol. 2023 Aug 31:13:1256882. doi: 10.3389/fcimb.2023.1256882. eCollection 2023.

Abstract

TRIM7 has been demonstrated to have significant roles in promoting host defense against viral infections and regulating immune signaling pathways. As an E3 ubiquitin ligase, it catalyzes the ubiquitination of various substrates, including adaptor proteins (MAVS and STING) and transcription factors (NF-κB and IRF3), thereby exerting positive or negative regulation on immune signal pathways. However, viruses have developed immune evasion mechanisms to counteract TRIM7. Some viruses can inhibit TRIM7 function by targeting it for degradation or sequestering it away from its targets. Moreover, TRIM7 may even facilitate viral infection by ubiquitinating viral proteins, including envelope proteins that are critical for tissue and species tropism. A comprehensive understanding of the interaction between TRIM7 and antiviral immunity is crucial for the development of innovative treatments for viral diseases.

Keywords: E3 ubiquitin ligase; MAVS; STING; TRIM7; enterovirus.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Immune Evasion
  • NF-kappa B
  • Tripartite Motif Proteins* / immunology
  • Ubiquitin-Protein Ligases* / immunology
  • Virus Diseases* / immunology

Substances

  • Adaptor Proteins, Signal Transducing
  • NF-kappa B
  • Ubiquitin-Protein Ligases
  • Tripartite Motif Proteins

Grants and funding

The authors declare financial support was received for the research, authorship, and/or publication of this article. This work was supported by grants from National Natural Science Foundation of China (82272306 and 82072270), College Students innovation and entrepreneurship training program of Shandong Province (S202210439011X), Taishan Scholars Program (tstp20221142), and Academic promotion programme of Shandong First Medical University (2019LJ001).