Researchers from Shanghai Medical College of Fudan University have recently revealed the reason why IFN-α is ineffective in patients with chronic hepatitis B (HBV) infection, confirming that HBV inhibits importin-α5 and protein kinase C-δ (proteinkinaseC-δ, PKC) -δ), attenuated IFN-α-induced STAT activation. Related papers were published in the Hepatology magazine (the latest impact factor 11.665) on February 5th. Leading this research is Professor Zhenghong Yuan, the deputy dean of Shanghai Medical College of Fudan University. It is mainly engaged in the research of molecular biology and immunology of hepatitis virus. In recent years, he has won the third prize of the National Natural Science Award, the third prize of the Shanghai Science and Technology Progress Award, the first prize of the Technical Invention Award of the Ministry of Education, the first prize of the Chinese Medicine and the third prize of the Shanghai Medical Science and Technology. Abstract: Hepatitis B, or hepatitis B for short, is a disease caused by hepatitis B virus (HBV) infecting the body. Recently, Fudan University's research on hepatitis B has achieved the latest results. According to the World Health Organization, about 2 billion people worldwide have been infected with HBV, of which 350 million people are chronically infected. China is a big country with hepatitis B, HBsAg carrying rate is 8-15%, and chronic HBV infection is the main cause of cirrhosis and hepatocellular carcinoma. Therefore, antiviral treatment is urgent. IFN-α is the first antiviral drug approved by the FDA for the treatment of hepatitis. However, the current IFN-α treatment is not effective for most patients with chronic hepatitis B virus (HBV) infection. Recent data indicate that HBV has evolved strategies to block nuclear transfer of signal transducers and transcription activator 1 (STAT1), limiting the cellular antiviral response induced by IFN-α. However, its specific molecular mechanism still needs further elucidation. In this article, the researchers reported that in human hepatocyte cell lines, HBV polymerase (Pol) expression inhibits the induction of IFN-stimulated genes, resulting in a reduction in IFN-α antiviral activity. The researchers confirmed that Pol ectopic expression inhibited IFN-α-induced phosphorylation of STAT1Ser727 and STAT1 / 2 nuclear aggregation, while phosphorylation of STAT1Tyr701 and STAT1-STAT2 heterodimer formation were not affected. Further research confirmed that Pol interacted with the catalytic domain of PKC-δ, disrupting the phosphorylation of PKC-δ and binding to STAT1, resulting in the inhibition of phosphorylation of STAT1Ser727. In addition, the researchers also found that Pol recruited the importin-α5 region of STAT1 / 2 through competitive binding, which interfered with the nuclear translocation of STAT1 / 2. Truncated analysis showed that Pol's terminal protein and RNaseH domain can bind to PKC-δ and importin-α5, respectively, and is responsible for inhibiting IFN-α signaling. More importantly, in the fluid dynamics-based HBV mouse model, the researchers confirmed the inhibition of STAT1 and PKC-δ phosphorylation and observed IFN in HBV cells from liver biopsies of patients with chronic hepatitis B. -α-induced STAT1 / 2 nuclear transfer is blocked. These results confirm that Pol plays an important role in HBV-mediated IFN-α signal antagonism, provides a possible molecular mechanism for HBV to resist IFN treatment and maintain HBV persistence.
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