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Volume 39 Issue 2
April 2024
    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
    shu

    Non-proteolytic ubiquitination of HBx controls HBV replication

    • 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

    • Highlights
      1. 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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    • Electronic Supplementary Material

      10.1016j.virs.2024.01.008-ESM.docx

      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.

      2. Dong H, Zhang L, Qian Z, Zhu X, Zhu G, Chen Y, Xie X, Ye Q, Zang J, Ren Z. 2015. Identification of hbv-mll4 integration and its molecular basis in chinese hepatocellular carcinoma. PloS one, 10:e0123175.

      3. Foss S, Watkinson R, Sandlie I, James LC, Andersen JT. 2015. Trim21:A cytosolic fc receptor with broad antibody isotype specificity. Immunol. Rev., 268:328-339.

      4. Keeble AH, Khan Z, Forster A, James LC. 2008. Trim21 is an igg receptor that is structurally, thermodynamically, and kinetically conserved. Proc Natl Acad Sci U S A, 105:6045-6050.

      5. Lamontagne RJ, Bagga S, Bouchard MJ. 2016. Hepatitis b virus molecular biology and pathogenesis. Hepatoma Res, 2:163-186.

      6. Li C, Han T, Guo R, Chen P, Peng C, Prag G, Hu R. 2020. An integrative synthetic biology approach to interrogating cellular ubiquitin and ufm signaling. Int. J. Mol. Sci., 21:4231.

      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.

      8. Nejepinska J, Malik R, Moravec M, Svoboda P. 2012. Deep sequencing reveals complex spurious transcription from transiently transfected plasmids. PloS one, 7:e43283.

      9. Nejepinska J, Malik R, Wagner S, Svoboda P. 2014. Reporters transiently transfected into mammalian cells are highly sensitive to translational repression induced by dsrna expression. PloS one, 9:e87517.

      10. Qi Z, Li G, Hu H, Yang C, Zhang X, Leng Q, Xie Y, Yu D, Zhang X, Gao Y. 2014. Recombinant covalently closed circular hepatitis b virus DNA induces prolonged viral persistence in immunocompetent mice. Virol. J., 88:8045-8056.

      11. Sheng X, Xia Z, Yang H, Hu R. 2023. The ubiquitin codes in cellular stress responses. Protein & Cell:pwad045.

      12. Sheng X, You Q, Zhu H, Li Q, Gao H, Wang H, You C, Meng Q, Nie Y, Zhang X. 2020. Enterohemorrhagic e. Coli effector nlel disrupts host nf-κb signaling by targeting multiple host proteins. J. Mol. Cell Biol, 12:318-321.

      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.

      14. Stepanenko AA, Heng HH. 2017. Transient and stable vector transfection:Pitfalls, off-target effects, artifacts. Mutat. Res.-Rev. Mutat. Res, 773:91-103.

      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.

      16. Yang L, Zou T, Chen Y, Zhao Y, Wu X, Li M, Du F, Chen Y, Xiao Z, Shen J. 2022. Hepatitis b virus x protein mediated epigenetic alterations in the pathogenesis of hepatocellular carcinoma. Hepatol. Int.:1-14.

      17. Zhang J-F, Xiong H-L, Cao J-L, Wang S-J, Guo X-R, Lin B-Y, Zhang Y, Zhao J-H, Wang Y-B, Zhang T-Y. 2018. A cell-penetrating whole molecule antibody targeting intracellular hbx suppresses hepatitis b virus via trim21-dependent pathway. Theranostics, 8:549.

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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
      • Received Date: 14 April 2023
      • Accepted Date: 24 January 2024

      Abstract: Highlights
      1. 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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