TRIM16 overexpression in HEK293T cells results in cell line-specific antiviral activity

ABSTRACT: In this paper we investigate one of the lesser studied TRIM family proteins, TRIM16, to determine if it might impact the ability of different viruses to replicate productively in host cells. TRIM16 is unique compared to other TRIM proteins in that it mediates E3 ligase activity despite lacking the catalytic RING domain present in other TRIM proteins. TRIM16 has been shown to play a role in innate immunity by increasing the secretion proinflammatory cytokine Il-1 in macrophages through interactions with components of the inflammasome complex (procaspase-1 and NALP-1). TRIM16 also mediates ubiquitination and aggregation of misfolded proteins which are subsequently degraded through the autophagic pathway in cells under proteotoxic and oxidative stress11. It does so through interactions with the p62-KEAP-NRF2 complex and stabilization of the NRF2 protein through multiple mechanisms11. Interestingly the NRF2 protein has been implicated in antiviral immunity, as previous studies have shown that infection of NRF2 (-/-) mice with respiratory syncytial virus (RSV) resulted in significantly higher viral titres in the lungs compared to NRF2 (+/+) mice. In addition to these clues in the literature, a recent study from our group examining transcriptional signatures in type II airway epithelial cells (AEC II) isolated from mock versus IAV-infected mice indicated that TRIM16 was upregulated in AECII following IAV infection in vivo.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Nichollas Scott  

LAB HEAD: Rubaiyea Farrukee

PROVIDER: PXD039241 | Pride | 2023-06-21

REPOSITORIES: Pride