TRIM Proteins in Antiviral Immunity and Virus Pathogenesis

Dear Colleagues,

Tripartite Motif (TRIM) proteins belong to a large family of E3-ubiquitin ligases, many of which have antiviral activity. TRIMs have long been known for their functions as direct restriction factors; however, they can also act indirectly by promoting the induction of antiviral type-I Interferons (IFN-I). TRIM activity has been linked to a variety of cellular functions, including the regulation of immune signaling, cell cycle, apoptosis, autophagy, and many others. Studies are uncovering unrecognized mechanisms of TRIM activity, including the direct ubiquitination of viral proteins that may balance proviral and antiviral functions, and may perform this via the synthesis of unconventional polyubiquitin chains. It is still unclear what mechanism balances the contradictory roles of TRIMs at the physiological level. The dual roles of TRIMs and their involvement in multiple cellular functions have made it virtually impossible to use them as feasible druggable targets. The generation of TRIM knockouts in cells and animals using CRISPR technology has led to an exponential advance in our understanding of TRIM functions. In this Special Issue, we will explore novel aspects of TRIM function in relation to virus infection, including proviral and antiviral roles, antagonism, and pathogenesis. New comprehensive studies may help identify novel strategies to modulate TRIM activity for therapeutic interventions.

Dr. Ricardo Rajsbaum
Guest Editor

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