Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Marios G. Koliopoulos, Mathilde Lethier, Annemarthe G. van der Veen, Kevin Haubrich, Janosch Hennig, Eva Kowalinski, Rebecca V. Stevens, Stephen R. Martin, Caetano Reis e Sousa, Stephen Cusack, Katrin Rittinger

ABSTRACT

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. More... »

PAGES

1820

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41467-018-04214-8

    DOI

    http://dx.doi.org/10.1038/s41467-018-04214-8

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1103771573

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/29739942


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