Citation: Xiangpeng Sheng, Yi Yang, Min Zhu, Linlin Zhou, Fang Zhu, Yuanfei Zhu, Siying Dong, Hui Kong, Honghua Wang, Ji Jiang, Mingyue Wan, Mingyang Feng, Qiang Deng, Yumin Xu, Qing You, Ronggui Hu. Non-proteolytic ubiquitination of HBx controls HBV replication .VIROLOGICA SINICA, 2024, 39(2) : 338-342.  http://dx.doi.org/10.1016/j.virs.2024.01.008

Non-proteolytic ubiquitination of HBx controls HBV replication

  • Highlights1. The expression level of TRIM21 in patients is negatively correlated with the replication and integration of HBV.2. TRIM21 was found to trigger non-proteolytic ubiquitination of X protein of HBV.3. This study proposes that the PRYSPRY and RING domains in TRIM21 dimer can form a docking conformation for HBx binding.4. TRIM21-mediated HBx ubiquitination disrupts the DDB1 recruitment to HBx and stabilize Smc6.

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    1. Decorsière A, Mueller H, Van Breugel PC, Abdul F, Gerossier L, Beran RK, Livingston CM, Niu C, Fletcher SP, Hantz O. 2016. Hepatitis b virus x protein identifies the smc5/6 complex as a host restriction factor. Nature, 531:386-389.

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    7. Mu T, Zhao X, Zhu Y, Fan H, Tang H. 2020. The e3 ubiquitin ligase trim21 promotes hbv DNA polymerase degradation. Viruses, 12:346.

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    13. Song Y, Li M, Wang Y, Zhang H, Wei L, Xu W. 2021. E3 ubiquitin ligase trim21 restricts hepatitis b virus replication by targeting hbx for proteasomal degradation. Antivir. Res., 192:105107.

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    15. van Breugel PC, Robert EI, Mueller H, Decorsière A, Zoulim F, Hantz O, Strubin M. 2012. Hepatitis b virus x protein stimulates gene expression selectively from extrachromosomal DNA templates. Hepatology, 56:2116-2124.

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    Non-proteolytic ubiquitination of HBx controls HBV replication

      Corresponding author: Xiangpeng Sheng, shengxiangpeng@ucas.ac.cn
      Corresponding author: Yumin Xu, xym121@163.com
      Corresponding author: Qing You, youqing@sjtu.edu.cn
      Corresponding author: Ronggui Hu, coryhu@sibcb.ac.cn
    • a. State Key Laboratory for Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China;
    • b. State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 200031, China;
    • c. Key Laboratory of Systems Health Science of Zhejiang Province, School of Life Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, China;
    • d. Department of Thoracic Surgery, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai 200025, China;
    • e. Shanghai Key Laboratory of Plant Molecular Sciences, College of Life Sciences, Shanghai Normal University, Shanghai 200234, China;
    • f. Department of Pathogenic Biology, West China School of Basic Medical Sciences & Forensic Medicine, Sichuan University, Chengdu 610041, China;
    • g. School of Medicine, Guizhou University, Guiyang 550025, China;
    • h. Key Laboratory of Medical Molecular Virology (MOE & MOH), School of Basic Medical Sciences, Fudan University, Shanghai 200032, China;
    • i. Department of Hospital Infection Management, Department of Infectious Diseases, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China;
    • j. School of Biomedical Engineering, Shanghai Jiao Tong University, Shanghai 200240, China

    Abstract: Highlights1. The expression level of TRIM21 in patients is negatively correlated with the replication and integration of HBV.2. TRIM21 was found to trigger non-proteolytic ubiquitination of X protein of HBV.3. This study proposes that the PRYSPRY and RING domains in TRIM21 dimer can form a docking conformation for HBx binding.4. TRIM21-mediated HBx ubiquitination disrupts the DDB1 recruitment to HBx and stabilize Smc6.

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