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Biochemistry IV - Biophysical Chemistry - Prof. Dr. Janosch Hennig

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New publication in Nature Communications

02.10.2024

Congratulations to Lucía and all of us who contributed to this exciting article published in Nature Communications. An amazing collaboration with Alfredo Castello’s lab at the Centre for Virus Research, University of Glasgow and with 8 other institutes in 5 countries (also special thanks to Fred Allain’s lab at ETH Zürich for sharing very important data derived from CLIR-MS/MS). Using a wide range of methods, combining biophysics with iCLIP2, fluorescence microscopy and viral fitness assays, we could show that structure- and sequence-specific RNA binding by TRIM25 is essential for TRIM25’s antiviral activity against human-pathogenic Sindbis virus. Lucía did an amazing job, doing most of the experiments and coordinating a large part of this study.
TRIM25_m9_mutant

This picture shows the dimeric molecular structure of TRIM25’s coiled-coil-PRYSPRY domain region, responsible for RNA binding. The RNA binding residues are highlighted. Mutating these leads to loss of RNA binding and antiviral activity.

 

 

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 & Janosch Hennig.

Press release of the University of Bayreuth: https://www.uni-bayreuth.de/en/press-release/trim25-immune-defense

Press release of EMBL Communications: https://www.embl.org/news/science-technology/the-cellular-superhero-that-protects-us-against-rna-viruses/

nature communications DOI: https://doi.org/10.1038/s41467-024-52918-x

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