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- W2772087653 abstract "Influenza A viruses (IAVs) take advantage of the host acetylation system for their own benefit. Whether the nucleoprotein (NP) of influenza A viruses undergoes acetylation and the interaction between the nucleoprotein and the class Ⅰ histone deacetylases were largely unknown. Here, we showed that the NP protein of IAV interacted with histone deacetylase 1 (HDAC1), which down-regulated the acetylation level of NP. Using mass spectrometry, we identified lysine 103(K103) as an acetylation site of the NP. Compared with wild-type protein, two K103 NP mutants, K103A and K103R, enhanced replication efficiency of the recombinant viruses in vitro. We further demonstrated that HDAC1 facilitated viral replication via two paths: promoting the nuclear retention of NP and inhibiting TBK1-IRF3 pathway. Our results lead to a new mechanism for regulating NP acetylation, indicating that HDAC1 may be a possible target for antiviral drugs." @default.
- W2772087653 created "2017-12-22" @default.
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- W2772087653 date "2017-12-12" @default.
- W2772087653 modified "2023-10-10" @default.
- W2772087653 title "Histone Deacetylase 1 Plays an Acetylation-Independent Role in Influenza A Virus Replication" @default.
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- W2772087653 doi "https://doi.org/10.3389/fimmu.2017.01757" @default.
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