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MINI REVIEW article
Front. Cell. Infect. Microbiol.
Sec. Virus and Host
Volume 15 - 2025 | doi: 10.3389/fcimb.2025.1573422
This article is part of the Research TopicImmunomodulatory Strategies for Managing Viral Infections: Host Immune response and therapeutic targetsView all articles
Insights into the protein domains of C-VI TRIM subfamily in viral infection
Provisionally accepted- 1China Medical University (Taiwan), Taichung, Taiwan
- 2Sinphar Pharmaceutical Co., Ltd., Sinphar Group, Yilan, Taiwan
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Tripartite motif (TRIM) proteins, defined by their conserved RBCC domain architecture, play key roles in various cellular processes and virus-host interactions. In this review, we focus on Class VI TRIM proteins, including TRIM24, TRIM28, and TRIM33, highlighting the distinct functional attributes of their RING, B-BOX1, B-BOX2, COILED COIL, PHD, and BRD domains in viral infection. Through multiple sequence alignment, we delineate both the conserved and divergent features within this subclass, underscoring the uniqueness of Class VI TRIM protein. Additionally, we explore the post-translational modifications (PTMs) of Class VI TRIM proteins including their functional differences in modulating viral infection. Moreover, we examine the C-VI TRIM protein complexes and their significant contributions to the antiviral response. Furthermore, we discuss small molecule ligands targeting Class VI TRIM domains, with a focus on druggable structural motifs. Understanding the multi-domain features of TRIM proteins is crucial for developing effective antiviral strategies and the therapeutic modulation of their activity.
Keywords: TRIM 28, trim24/trim28/trim33 complex, RBCC domain, C VI TRIM PROTEINS, TRIM24, Trim33, virus
Received: 09 Feb 2025; Accepted: 16 Apr 2025.
Copyright: © 2025 Patrick, Lo and Su. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Wen-Chi Su, China Medical University (Taiwan), Taichung, Taiwan
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