Abstract
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The expression level of TRIM21 in patients is negatively correlated with the replication and integration of HBV.
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TRIM21 was found to trigger non-proteolytic ubiquitination of X protein of HBV.
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This study proposes that the PRYSPRY and RING domains in TRIM21 dimer can form a docking conformation for HBx binding.
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TRIM21-mediated HBx ubiquitination disrupts the DDB1 recruitment to HBx and stabilize Smc6.
MeSH terms
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Hepatitis B virus* / genetics
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Hepatitis B virus* / physiology
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Host-Pathogen Interactions
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Humans
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Trans-Activators* / genetics
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Trans-Activators* / metabolism
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Ubiquitination*
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Viral Regulatory and Accessory Proteins* / genetics
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Viral Regulatory and Accessory Proteins* / metabolism
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Virus Replication*
Substances
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Viral Regulatory and Accessory Proteins
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hepatitis B virus X protein
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Trans-Activators