The molecular dissection of TRIM25’s RNA-binding mechanism provides key insights into its antiviral activity

Lucía Álvarez, Kevin Haubrich, Louisa Iselin, Laurent Gillioz, Vincenzo Ruscica, Karine Lapouge, Sandra Augsten, Ina Huppertz, Nila Roy Choudhury, Bernd Simon, Pawel Masiewicz, Mathilde Lethier, Stephen Cusack, Katrin Rittinger, Frank Gabel, Alexander Leitner, Gracjan Michlewski, Matthias W. Hentze, Frédéric H. T. Allain, Alfredo Castello () and Janosch Hennig ()
Additional contact information
Lucía Álvarez: European Molecular Biology Laboratory (EMBL) Heidelberg
Kevin Haubrich: European Molecular Biology Laboratory (EMBL) Heidelberg
Louisa Iselin: University of Oxford
Laurent Gillioz: ETH Zürich
Vincenzo Ruscica: 464 Bearsden Road
Karine Lapouge: European Molecular Biology Laboratory (EMBL) Heidelberg
Sandra Augsten: European Molecular Biology Laboratory (EMBL) Heidelberg
Ina Huppertz: European Molecular Biology Laboratory (EMBL) Heidelberg
Nila Roy Choudhury: International Institute of Molecular and Cell Biology in Warsaw
Bernd Simon: European Molecular Biology Laboratory (EMBL) Heidelberg
Pawel Masiewicz: European Molecular Biology Laboratory (EMBL) Heidelberg
Mathilde Lethier: 38042 Grenoble Cedex 9
Stephen Cusack: 38042 Grenoble Cedex 9
Katrin Rittinger: 1 Midland Road
Frank Gabel: Direction de la Recherche Fondamentale, Institut de Biologie Structurale, Grenoble, France; Centre National de la Recherche Scientifique, Institut de Biologie Structurale
Alexander Leitner: 8093
Gracjan Michlewski: International Institute of Molecular and Cell Biology in Warsaw
Matthias W. Hentze: European Molecular Biology Laboratory (EMBL) Heidelberg
Frédéric H. T. Allain: ETH Zürich
Alfredo Castello: 464 Bearsden Road
Janosch Hennig: European Molecular Biology Laboratory (EMBL) Heidelberg

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-52918-x

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