Degradation of ACSL3 by influenza A virus shifts unfolded protein response from antiviral defense to viral evasion

Shuoxuan Zhao; Yichao Chen; Tianxin Zhang; Yaoyao Gao; Jing Wu; Fangji Yang; Yongxiang Liu; Xuesong Liu; Nan Qi

doi:10.1016/j.virs.2026.06.008

June 2026

Citation: Shuoxuan Zhao, Yichao Chen, Tianxin Zhang, Yaoyao Gao, Jing Wu, Fangji Yang, Yongxiang Liu, Xuesong Liu, Nan Qi. Degradation of ACSL3 by influenza A virus shifts unfolded protein response from antiviral defense to viral evasion .VIROLOGICA SINICA, 2026, 41(3) : 638-650. http://dx.doi.org/10.1016/j.virs.2026.06.008

Degradation of ACSL3 by influenza A virus shifts unfolded protein response from antiviral defense to viral evasion

Shuoxuan Zhao ^a ,
Yichao Chen ^a,b ,
Tianxin Zhang ^b ,
Yaoyao Gao ^b ,
Jing Wu ^a ,
Fangji Yang ^a ,
Yongxiang Liu ^{a,b
,,} ,
Xuesong Liu ^{a
,,} ,
Nan Qi ^{a,b
,,}

a. State Key Laboratory of Respiratory Disease, The First Affiliated Hospital of Guangzhou Medical University, Guangzhou Medical University, Guangzhou 510120, China;
b. Guangzhou National Laboratory, Guangzhou International Bio-Island, Guangzhou 510005, China

Corresponding author: Yongxiang Liu, liu_yongxiang@gzlab.ac.cn
Xuesong Liu, liuxuesong1000@sina.com
Nan Qi, qi_nan@gzlab.ac.cn
Received Date: 12 April 2026
Accepted Date: 09 June 2026
Available online: 13 June 2026

Abstract

Host restriction factors and viral evasion strategies involved in the virus-host arms races remain to be discovered. Through an initial membrane protein-targeted CRISPR-Cas9 screening, we identified Acyl-CoA synthetase long-chain family member 3 (ACSL3) as a restriction factor against influenza A virus (IAV). Clinical transcriptomic analysis shows that ACSL3 is upregulated in peripheral blood mononuclear cells from mildly ill patients with influenza. Ectopic expression and loss-of-function validation demonstrate the physiological role of ACSL3 in restricting viral proliferation of diverse IAV subtypes (H1N1, H3N2, H3N8) in vitro and in vivo. Mechanistically, ACSL3 potentiates the antiviral unfolded protein response (UPR) by engaging the endoplasmic reticulum (ER) stress sensors IRE1α and PERK, thereby enhancing the IRE1α-XBP1-s driven inflammation and inhibiting the PERK-ATF4-CHOP mediated apoptosis. Conversely, IAV triggers the lysosomal degradation of ACSL3 and thus reprograms UPR to promote an immunologically silent apoptosis for viral egress and dissemination. Our findings establish ACSL3 as a molecular switch balancing the UPR-mediated antiviral response, and reveal a targeted viral evasion strategy in the virus-host interplay.
- Influenza A virus (IAV)
- , ACSL3
- , Unfolded protein response (UPR)
- , Endoplasmic reticulum stress (ER stress)
- , Apoptosis

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