These authors contributed equally to this work.
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Viral Hepatitis
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Tripartite motif-containing 22 inhibits the activity of hepatitis B virus core promoter, which is dependent on nuclear-located RING domain†
Article first published online: 6 APR 2009
DOI: 10.1002/hep.23011
Copyright © 2009 American Association for the Study of Liver Diseases
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How to Cite
Gao, B., Duan, Z., Xu, W. and Xiong, S. (2009), Tripartite motif-containing 22 inhibits the activity of hepatitis B virus core promoter, which is dependent on nuclear-located RING domain. Hepatology, 50: 424–433. doi: 10.1002/hep.23011
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Potential conflict of interest: Nothing to report.
Publication History
- Issue published online: 29 JUL 2009
- Article first published online: 6 APR 2009
- Accepted manuscript online: 6 APR 2009 12:00AM EST
- Manuscript Accepted: 26 MAR 2009
- Manuscript Received: 23 NOV 2008
Funded by
- National Natural Science Foundation of China. Grant Numbers: 30872355, 30890141
- Major State Basic Research Development Program of China. Grant Number: 2007CB512401
- Shanghai STCSM. Grant Numbers: 07QA14005, 08JC1401200
- China 863. Grant Number: 2006AA02Z403
- Program for Outstanding Medical Academic Leader. Grant Number: LJ06011
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Abstract
Members of the tripartite motif (TRIM) family are a part of the innate immune system to counter intracellular pathogens. TRIM22 has been reported to possess antiretroviral activity. Here we report that TRIM22 is involved in antiviral immunity against hepatitis B virus (HBV). Our results showed that TRIM22, being a strongly induced gene by interferons in human hepatoma HepG2 cells, could inhibit HBV gene expression and replication in a cell culture system as well as in a mouse model system. Importantly, it was found that TRIM22 could inhibit the activity of HBV core promoter (CP) in a dose-dependent manner. However, TRIM22 lacking the C terminal SPRY domain lost this activity. Further study showed that the SPRY domain deletion mutant was localized exclusively to the cytoplasm of HepG2 cells. In contrast, the wild-type TRIM22 was localized to the nucleus, as expected for a transcriptional suppressor. Interestingly, although RING domain mutants of TRIM22 were localized to the nucleus, they could not inhibit HBV CP activity, indicating that TRIM22-mediated anti-HBV activity was dependent on the nuclear-located RING domain. Conclusion: These findings suggest that TRIM22, which exhibits anti-HBV activity by acting as a transcriptional suppressor, may play an important role in the clearance of HBV. (HEPATOLOGY 2009.)