Journal
CELLULAR MICROBIOLOGY
Volume 19, Issue 2, Pages -Publisher
WILEY
DOI: 10.1111/cmi.12643
Keywords
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Categories
Funding
- Key Research Program of the Chinese Academy of Sciences [KSZD-EW-Z-005-001]
- China Ministry of Science and Technology (MOST) Project 973 [2012CB955501]
- National Natural Science Foundation of China (NSFC) [31572526, 31402216, 81271849, 31472178]
- National Twelfth Five-Year Plan for Science & Technology Support [2015BAD11B02]
- National Key Research Program [2016YFD0500206]
- Innovative Research Group of National Natural Science Foundation of China [81321063]
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Influenza A virus evades host antiviral defense through hijacking innate immunity by its non-structural protein 1 (NS1). By using mass spectrometry, threonine 80 (T80) was identified as a novel phosphorylated residue in the NS1 of the influenza virus A/WSN/1933(H1N1). By generating recombinant influenza viruses encoding NS1 T80 mutants, the roles of this phosphorylation site were characterized during viral replication. The T80E (phosphomimetic) mutant attenuated virus replication, whereas the T80A (non-phosphorylatable) mutant did not. Similar phenotypes were observed for these mutants in a mouse model experiment. In further study, the T80E mutant decreased the binding capacity between NS1 and viral nucleoprotein (NP), leading to impaired viral ribonucleoprotein (vRNP)-mediated viral transcription. The T80E mutant was also unable to inhibit interferon (IFN) production by reducing the binding affinity between NS1 and retinoic acid-induced gene 1 protein (RIG-I), causing attenuation of virus replication. Taken together, the present study reveals that T80 phosphorylation of NS1 reduced influenza virus replication through controlling RIG-I-mediated IFN production and vRNP activity.
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