Key result
Class VI TRIM proteins regulate viral infections and host antiviral responses via unique multi-domain architecture.
Why the study?
The distinct functional attributes and post-translational modifications of Class VI TRIM proteins in viral infection and their therapeutic potential require comprehensive understanding.
Understanding the multi-domain features of Class VI TRIM proteins provides insights for developing effective antiviral strategies.
Class VI TRIM domains may guide antiviral target discovery; leaves open clinical translation from molecular alignments.
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.
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Patrick et al. (2025) conducted a review in Viral infection. Class VI TRIM proteins (TRIM24, TRIM28, TRIM33) was evaluated. Class VI TRIM proteins, including TRIM24, TRIM28, and TRIM33, utilize their unique multi-domain architecture to regulate viral infections and host antiviral responses.
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