SARS-CoV-2 NSP13 Inhibits Type I IFN Production by Degradation of TBK1 via p62-Dependent Selective Autophagy.
Chao SuiTong-Yang XiaoShengyuan ZhangHongxiang ZengYi ZhengBingyu LiuGang XuChengjiang GaoZheng ZhangPublished in: Journal of immunology (Baltimore, Md. : 1950) (2022)
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which causes coronavirus disease 2019 (COVID-19), has seriously threatened global public health. Severe COVID-19 has been reported to be associated with an impaired IFN response. However, the mechanisms of how SARS-CoV-2 antagonizes the host IFN response are poorly understood. In this study, we report that SARS-CoV-2 helicase NSP13 inhibits type I IFN production by directly targeting TANK-binding kinase 1 (TBK1) for degradation. Interestingly, inhibition of autophagy by genetic knockout of Beclin1 or pharmacological inhibition can rescue NSP13-mediated TBK1 degradation in HEK-293T cells. Subsequent studies revealed that NSP13 recruits TBK1 to p62, and the absence of p62 can also inhibit TBK1 degradation in HEK-293T and HeLa cells. Finally, TBK1 and p62 degradation and p62 aggregation were observed during SARS-CoV-2 infection in HeLa-ACE2 and Calu3 cells. Overall, our study shows that NSP13 inhibits type I IFN production by recruiting TBK1 to p62 for autophagic degradation, enabling it to evade the host innate immune response, which provides new insights into the transmission and pathogenesis of SARS-CoV-2 infection.
Keyphrases
- sars cov
- respiratory syndrome coronavirus
- immune response
- coronavirus disease
- cell cycle arrest
- cell death
- dendritic cells
- public health
- induced apoptosis
- endoplasmic reticulum stress
- oxidative stress
- signaling pathway
- cancer therapy
- dna methylation
- cell proliferation
- pi k akt
- transcription factor
- single cell
- binding protein
- tyrosine kinase