The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity
Year: 2024
Type: article
Abstract: TRIM25 is an RNA-binding ubiquitin E3 ligase with central but poorly understood roles in the innate immune response to RNA viruses. The link between TRIM25's RNA binding and its role in innate immunity has not been established. Thus, we utilized a multitude of biophysical techniques to identify key RNA-binding residues of TRIM25 and developed an RNA-binding deficient mutant (TRIM25-m9). Using iCLIP2 in virus-infected and uninfected cells, we identified TRIM25's RNA sequence and structure specificity, that it binds specifically to viral RNA, and that the interaction with RNA is critical for its antiviral activity.
Authors: Álvarez, Lucía, Haubrich, Kevin, Iselin, Louisa, Gillioz, Laurent, Ruscica, Vincenzo, Lapouge, Karine, Augsten, Sandra, Huppertz, Ina, Choudhury, Nila Roy, Simon, Bernd, Masiewicz, Pawel, Lethier, Mathilde, Cusack, Stephen, Rittinger, Katrin, Gabel, Frank, Leitner, Alexander, Michlewski, Gracjan, Hentze, Matthias W., Allain, Frédéric H.T., Castello, Alfredo, Henning, Janosch
Language: English
Subfield: Immunology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W6947401087
FWCI:
Cites:
Cited by:
Related to: