tetano
Editor, Senior Moderator
Antiviral Res
. 2024 Jun 27:228:105925.
doi: 10.1016/j.antiviral.2024.105925. Online ahead of print. hnRNPAB inhibits Influenza A virus infection by disturbing polymerase activity
Linyue Lv[SUP] 1 [/SUP], Xue Yang[SUP] 1 [/SUP], Yuelan Zhang[SUP] 1 [/SUP], Xiaoyan Ren[SUP] 1 [/SUP], Shaowei Zeng[SUP] 1 [/SUP], Zhuyou Zhang[SUP] 1 [/SUP], Qinyang Wang[SUP] 1 [/SUP], Jiaxi Lv[SUP] 2 [/SUP], Pengyue Gao[SUP] 3 [/SUP], Martin E Dorf[SUP] 4 [/SUP], Shitao Li[SUP] 5 [/SUP], Ling Zhao[SUP] 6 [/SUP], Bishi Fu[SUP] 7 [/SUP]
Affiliations
Influenza A virus (IAV) continuously poses a considerable threat to global health through seasonal epidemics and recurring pandemics. IAV RNA-dependent RNA polymerases (FluPol) mediate the transcription of RNA and replication of the viral genome. Searching for targets that inhibit viral polymerase activity helps us develop better antiviral drugs. Here, we identified heterogeneous nuclear ribonucleoprotein A/B (hnRNPAB) as an anti-influenza host factor. hnRNPAB interacts with NP of IAV to inhibit the interaction between PB1 and NP, which is dependent on the 5-amino-acid peptide of the hnRNPAB C-terminal domain (aa 318-322). We further found that the 5-amino-acid peptide blocks the interaction between PB1 and NP to destroy the FluPol activity. In vivo studies demonstrate that hnRNPAB-deficient mice display higher viral burdens, enhanced cytokine production, and increased mortality after influenza infection. These data demonstrate that hnRNPAB perturbs FluPol complex conformation to inhibit IAV infection, providing insights into anti-influenza defense mechanisms.
Keywords: Antiviral; FluPol; Influenza a virus; hnRNPAB.
. 2024 Jun 27:228:105925.
doi: 10.1016/j.antiviral.2024.105925. Online ahead of print. hnRNPAB inhibits Influenza A virus infection by disturbing polymerase activity
Linyue Lv[SUP] 1 [/SUP], Xue Yang[SUP] 1 [/SUP], Yuelan Zhang[SUP] 1 [/SUP], Xiaoyan Ren[SUP] 1 [/SUP], Shaowei Zeng[SUP] 1 [/SUP], Zhuyou Zhang[SUP] 1 [/SUP], Qinyang Wang[SUP] 1 [/SUP], Jiaxi Lv[SUP] 2 [/SUP], Pengyue Gao[SUP] 3 [/SUP], Martin E Dorf[SUP] 4 [/SUP], Shitao Li[SUP] 5 [/SUP], Ling Zhao[SUP] 6 [/SUP], Bishi Fu[SUP] 7 [/SUP]
Affiliations
- PMID: 38944160
- DOI: 10.1016/j.antiviral.2024.105925
Influenza A virus (IAV) continuously poses a considerable threat to global health through seasonal epidemics and recurring pandemics. IAV RNA-dependent RNA polymerases (FluPol) mediate the transcription of RNA and replication of the viral genome. Searching for targets that inhibit viral polymerase activity helps us develop better antiviral drugs. Here, we identified heterogeneous nuclear ribonucleoprotein A/B (hnRNPAB) as an anti-influenza host factor. hnRNPAB interacts with NP of IAV to inhibit the interaction between PB1 and NP, which is dependent on the 5-amino-acid peptide of the hnRNPAB C-terminal domain (aa 318-322). We further found that the 5-amino-acid peptide blocks the interaction between PB1 and NP to destroy the FluPol activity. In vivo studies demonstrate that hnRNPAB-deficient mice display higher viral burdens, enhanced cytokine production, and increased mortality after influenza infection. These data demonstrate that hnRNPAB perturbs FluPol complex conformation to inhibit IAV infection, providing insights into anti-influenza defense mechanisms.
Keywords: Antiviral; FluPol; Influenza a virus; hnRNPAB.