Journal article

Identification of a second binding site on the TRIM25 B30.2 domain

Akshay A D'Cruz, Nadia J Kershaw, Thomas J Hayman, Edmond M Linossi, Jessica J Chiang, May K Wang, Laura F Dagley, Tatiana B Kolesnik, Jian-Guo Zhang, Seth L Masters, Michael DW Griffin, Michaela U Gack, James M Murphy, Nicos A Nicola, Jeffrey J Babon, Sandra E Nicholson

BIOCHEMICAL JOURNAL | PORTLAND PRESS LTD | Published : 2018

Abstract

The retinoic acid-inducible gene-I (RIG-I) receptor recognizes short 5'-di- and triphosphate base-paired viral RNA and is a critical mediator of the innate immune response against viruses such as influenza A, Ebola, HIV and hepatitis C. This response is reported to require an orchestrated interaction with the tripartite motif 25 (TRIM25) B30.2 protein-interaction domain. Here, we present a novel second RIG-I-binding interface on the TRIM25 B30.2 domain that interacts with CARD1 and CARD2 (caspase activation and recruitment domains) of RIG-I and is revealed by the removal of an N-terminal α-helix that mimics dimerization of the full-length protein. Further characterization of the TRIM25 coile..

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Grants

Awarded by National Health and Medical Research Council (NHMRC), Australia


Awarded by U.S. National Institutes of Health


Awarded by NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES


Funding Acknowledgements

This work was supported, in part, by the National Health and Medical Research Council (NHMRC), Australia [program grant #461219, project grant #637348 and program grant #1016647], an NHMRC IRIISS grant and a Victorian State Government Operational Infrastructure Scheme grant, as well as the U.S. National Institutes of Health [grant number R01 AI087846 (to M.U.G.)]. S.E.N., J.J.B., J.M.M. and N.A.N. were supported by NHMRC fellowships. A.A.D. and E.M.L. were supported by Australian Postgraduate Awards.