at Google ScholarTitle data
Koliopoulos, Marios G. ; Lethier, Mathilde ; van der Veen, Annemarthe G. ; Haubrich, Kevin ; Hennig, Janosch ; Kowalinski, Eva ; Stevens, Rebecca V. ; Martin, Stephen R. ; Reis e Sousa, Caetano ; Cusack, Stephen ; Rittinger, Katrin:
Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition.
In: Nature Communications.
Vol. 9
(2018)
.
- 1820.
ISSN 2041-1723
DOI: https://doi.org/10.1038/s41467-018-04214-8
Abstract in another language
RIG-I is a viral RNA sensor that induces the production of type I interferon (IFN) in response to infection with a variety of viruses. Modification of RIG-I with K63-linked poly-ubiquitin chains, synthesised by TRIM25, is crucial for activation of the RIG-I/MAVS signalling pathway. TRIM25 activity is targeted by influenza A virus non-structural protein 1 (NS1) to suppress IFN production and prevent an efficient host immune response. Here we present structures of the human TRIM25 coiled-coil-PRYSPRY module and of complexes between the TRIM25 coiled-coil domain and NS1. These structures show that binding of NS1 interferes with the correct positioning of the PRYSPRY domain of TRIM25 required for substrate ubiquitination and provide a mechanistic explanation for how NS1 suppresses RIG-I ubiquitination and hence downstream signalling. In contrast, the formation of unanchored K63-linked poly-ubiquitin chains is unchanged by NS1 binding, indicating that RING dimerisation of TRIM25 is not affected by NS1.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry > Chair Biochemistry IV - Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry Research Institutions > Central research institutes > Nordbayerisches Zentrum für NMR-Spektroskopie - NMR-Zentrum Research Institutions Research Institutions > Central research institutes |
| Result of work at the UBT: | No |
| DDC Subjects: | 500 Science > 540 Chemistry 500 Science > 570 Life sciences, biology |
| Date Deposited: | 07 Oct 2021 07:20 |
| Last Modified: | 21 Nov 2024 14:20 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/67220 |