Journal
JOURNAL OF VIROLOGY
Volume 88, Issue 17, Pages 10252-10258Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00869-14
Keywords
-
Categories
Funding
- National Natural Sciences Foundation of China [31225027, 31121004]
- National Basic Research Program (973) of China [2014CB522700]
- Fundamental Research Funds for the Central Universities [2013PY043]
- U.S. National Institutes of Health [AI069285]
Ask authors/readers for more resources
NEMO (NF-kappa B essential modulator) is a bridging adaptor indispensable for viral activation of interferon (IFN) antiviral response. Herein, we show that hepatitis A virus (HAV) 3C protease (3C(pro)) cleaves NEMO at the Q304 residue, negating its signaling adaptor function and abrogating viral induction of IFN-beta synthesis via the retinoic acid-inducible gene I/melanoma differentiation-associated protein 5 (RIG-I/MDA5) and Toll-like receptor 3 (TLR3) pathways. NEMO cleavage and IFN antagonism, however, were lost upon ablation of the catalytic activity of 3C(pro). These data describe a novel immune evasion mechanism of HAV.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available
Share Paper
