The Role of TRIM Proteins in Antiviral Defense
DOI:
https://doi.org/10.54097/a127xa83Keywords:
TRIM proteins; ubiquitination; pathogenesis.Abstract
The Tripartite motif (TRIM) protein family is classified among a cohort of E3 ubiquitin ligase families. A large percentage of TRIM proteins are E3 ubiquitin ligase active and take part in a number of cellular functions. By adding ubiquitin molecules to target proteins via a variety of techniques, it can change those proteins. The important role of the TRIM protein in controlling pattern recognition receptor signaling pathways and the defense mechanisms of mammals against viruses, with a focus on protecting the host from viral infections, has been clarified by recent study. In addition to triggering crucial cell-intrinsic defense mechanisms like autophagy and transcription-dependent antiviral responses, TRIM proteins can also exhibit direct antiviral effects by obstructing particular viral components via a variety of mechanisms. Regrettably, certain viruses have developed efficient mechanisms to evade the antiviral activities exerted by specific TRIM proteins, including SARS-CoV-2. Viruses has the capacity to exploit TRIMs and the ubiquitination process directly, hence enhancing the viral replication cycle and inducing heightened pathogenicity. In this article, I have delved into research that explores the molecular mechanisms responsible for the antiviral effects of TRIM proteins. Additionally, I have examined how TRIM proteins exert their influence on various viral entities, shedding light on their crucial role in the immune response against viral infections.
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