Articles

Herpes simplex virus 2 (HSV-2) is a considerable global strain, responsible for serious morbidity and mortality, especially among women, oppressed communities, and those who engage in high-risk sexual behavior. The tripartite motif (TRIM) proteins, a family of E3 ubiquitin ligase, play a considerable role in regulating antiviral immunity against HSV-2. TRIM26, a member of the TRIM protein family, has been shown to engage with IRF3, regulating interferon production and maintaining a balanced immune response. Recent findings have revealed that TRIM26 can trigger the ubiquitination of proteins affiliated with HSV-2 replication, leading to the degradation of viral proteins and regulate the viral replication. Furthermore, TRIM26 can negatively regulate key immune pathways. Other TRIM proteins, such as TRIM5α , TRIM23, and TRIM34, also have been linked in immune response against HSV-1. This review highlights the complex interaction between TRIM proteins and HSV-2, underscoring their potential as therapeutic targets for combating viral infectious diseases. Further exploration into the molecular mechanisms of TRIM proteins may lead to the breakthrough of novel therapeutic approaches against HSV and other viral pathogens.