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Article: HBV X protein mutations affect HBV transcription and association of histone-modifying enzymes with covalently closed circular DNA

TitleHBV X protein mutations affect HBV transcription and association of histone-modifying enzymes with covalently closed circular DNA
Authors
Issue Date2020
PublisherNature Research (part of Springer Nature): Fully open access journals. The Journal's web site is located at http://www.nature.com/srep/index.html
Citation
Scientific Reports, 2020, v. 10, p. article no. 802 How to Cite?
AbstractThe hepatitis B X protein (HBx) plays a role in the epigenetic regulation of hepatitis B virus (HBV) replication. This study investigated the effects of HBx mutations on HBV transcription and the recruitment of HBx, histone acetyl-transferase P300 and histone deacetylase 1 (HDAC1) to circularized HBV DNA (which resembles covalently closed circular DNA [cccDNA]). Compared with wild type, majority of mutants had lower levels of intracellular HBV RNA (44–77% reduction) and secretory HBsAg (25–81% reduction), and 12 mutants had a reduction in intracellular encapsidated HBV DNA (33–64% reduction). Eight mutants with >70% reduction in HBV RNA and/or HBsAg were selected for chromatin immunoprecipitation analysis. Four HBx mutants with mutations in amino acid residues 55–60 and 121–126 had a lower degree of HBx-cccDNA association than wild type HBx (mean % input: 0.02–0.64% vs. 3.08% in wild type). A reduced association between cccDNA and P300 (mean % input: 0.69–1.81% vs. 3.48% in wild type) and an augmented association with HDAC1 (mean % input: 4.01–14.0% vs. 1.53% in wild type) were detected. HBx amino acid residues 55–60 and 121–126 may play an important role in HBV transcription regulation, via their impeded interaction with cccDNA and altered recruitment of histone modifying enzymes to cccDNA.
Persistent Identifierhttp://hdl.handle.net/10722/280419
ISSN
2019 Impact Factor: 3.998
2015 SCImago Journal Rankings: 2.073
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorCHONG, CK-
dc.contributor.authorCheng, CYS-
dc.contributor.authorTsoi, SYJ-
dc.contributor.authorHuang, F-Y-
dc.contributor.authorLIU, F-
dc.contributor.authorFung, J-
dc.contributor.authorSeto, W-K-
dc.contributor.authorLai, KK-Y-
dc.contributor.authorLai, C-L-
dc.contributor.authorYuen, R-M-
dc.contributor.authorWong, DK-H-
dc.date.accessioned2020-02-07T07:40:40Z-
dc.date.available2020-02-07T07:40:40Z-
dc.date.issued2020-
dc.identifier.citationScientific Reports, 2020, v. 10, p. article no. 802-
dc.identifier.issn2045-2322-
dc.identifier.urihttp://hdl.handle.net/10722/280419-
dc.description.abstractThe hepatitis B X protein (HBx) plays a role in the epigenetic regulation of hepatitis B virus (HBV) replication. This study investigated the effects of HBx mutations on HBV transcription and the recruitment of HBx, histone acetyl-transferase P300 and histone deacetylase 1 (HDAC1) to circularized HBV DNA (which resembles covalently closed circular DNA [cccDNA]). Compared with wild type, majority of mutants had lower levels of intracellular HBV RNA (44–77% reduction) and secretory HBsAg (25–81% reduction), and 12 mutants had a reduction in intracellular encapsidated HBV DNA (33–64% reduction). Eight mutants with >70% reduction in HBV RNA and/or HBsAg were selected for chromatin immunoprecipitation analysis. Four HBx mutants with mutations in amino acid residues 55–60 and 121–126 had a lower degree of HBx-cccDNA association than wild type HBx (mean % input: 0.02–0.64% vs. 3.08% in wild type). A reduced association between cccDNA and P300 (mean % input: 0.69–1.81% vs. 3.48% in wild type) and an augmented association with HDAC1 (mean % input: 4.01–14.0% vs. 1.53% in wild type) were detected. HBx amino acid residues 55–60 and 121–126 may play an important role in HBV transcription regulation, via their impeded interaction with cccDNA and altered recruitment of histone modifying enzymes to cccDNA.-
dc.languageeng-
dc.publisherNature Research (part of Springer Nature): Fully open access journals. The Journal's web site is located at http://www.nature.com/srep/index.html-
dc.relation.ispartofScientific Reports-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleHBV X protein mutations affect HBV transcription and association of histone-modifying enzymes with covalently closed circular DNA-
dc.typeArticle-
dc.identifier.emailCheng, CYS: serenecy@hku.hk-
dc.identifier.emailHuang, F-Y: fungyu@hkucc.hku.hk-
dc.identifier.emailFung, J: jfung@hkucc.hku.hk-
dc.identifier.emailSeto, W-K: wkseto@hku.hk-
dc.identifier.emailLai, C-L: hrmelcl@hkucc.hku.hk-
dc.identifier.emailYuen, R-M: mfyuen@hku.hk-
dc.identifier.emailWong, DK-H: danywong@hku.hk-
dc.identifier.authorityFung, J=rp00518-
dc.identifier.authoritySeto, W-K=rp01659-
dc.identifier.authorityLai, C-L=rp00314-
dc.identifier.authorityYuen, R-M=rp00479-
dc.identifier.authorityWong, DK-H=rp00492-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1038/s41598-020-57637-z-
dc.identifier.pmid31964944-
dc.identifier.pmcidPMC6972884-
dc.identifier.scopuseid_2-s2.0-85078143241-
dc.identifier.hkuros309083-
dc.identifier.volume10-
dc.identifier.spagearticle no. 802-
dc.identifier.epagearticle no. 802-
dc.publisher.placeUnited Kingdom-

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