SIRT7 restricts HBV transcription and replication through catalyzing desuccinylation of histone H3 associated with cccDNA minichromosome

Chronic hepatitis B virus (HBV) infection is a significant public health burden worldwide. HBV covalently closed circular DNA (cccDNA) organized as a minichromosome in nucleus is responsible for viral persistence and is the key obstacle for a cure of chronic hepatitis B (CHB). Recent studies suggest...

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Published inClinical science (1979) Vol. 135; no. 12; pp. 1505 - 1522
Main Authors Yu, Hai-Bo, Cheng, Sheng-Tao, Ren, Fang, Chen, Yong, Shi, Xiao-Feng, Wong, Vincent Kam Wai, Law, Betty Yuen Kwan, Ren, Ji-Hua, Zhong, Shan, Chen, Wei-Xian, Xu, Hong-Mei, Zhang, Zhen-Zhen, Hu, Jie-Li, Cai, Xue-Fei, Hu, Yuan, Zhang, Wen-Lu, Long, Quan-Xin, He, Lin, Hu, Zhong-Wen, Jiang, Hui, Zhou, Hong-Zhong, Huang, Ai-Long, Chen, Juan
Format Journal Article
LanguageEnglish
Published 25.06.2021
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Abstract Chronic hepatitis B virus (HBV) infection is a significant public health burden worldwide. HBV covalently closed circular DNA (cccDNA) organized as a minichromosome in nucleus is responsible for viral persistence and is the key obstacle for a cure of chronic hepatitis B (CHB). Recent studies suggest cccDNA transcription is epigenetically regulated by histone modifications, especially histone acetylation and methylation. In the present study, we identified transcriptionally active histone succinylation (H3K122succ) as a new histone modification on cccDNA minichromosome by using cccDNA ChIP-Seq approach. Silent mating type information regulation 2 homolog 7 (SIRT7), as an NAD+-dependent histone desuccinylase, could bind to cccDNA through interaction with HBV core protein where it catalyzed histone 3 lysine 122 (H3K122) desuccinylation. Moreover, SIRT7 acts cooperatively with histone methyltransferase, suppressor of variegation 3–9 homolog 1 (SUV39H1) and SET domain containing 2 (SETD2) to induce silencing of HBV transcription through modulation of chromatin structure. Our data improved the understanding of histone modifications of the cccDNA minichromosome, thus transcriptional silencing of cccDNA may represent a novel antiviral strategy for the prevention or treatment of HBV infection.
AbstractList Chronic hepatitis B virus (HBV) infection is a significant public health burden worldwide. HBV covalently closed circular DNA (cccDNA) organized as a minichromosome in nucleus is responsible for viral persistence and is the key obstacle for a cure of chronic hepatitis B (CHB). Recent studies suggest cccDNA transcription is epigenetically regulated by histone modifications, especially histone acetylation and methylation. In the present study, we identified transcriptionally active histone succinylation (H3K122succ) as a new histone modification on cccDNA minichromosome by using cccDNA ChIP-Seq approach. Silent mating type information regulation 2 homolog 7 (SIRT7), as an NAD+-dependent histone desuccinylase, could bind to cccDNA through interaction with HBV core protein where it catalyzed histone 3 lysine 122 (H3K122) desuccinylation. Moreover, SIRT7 acts cooperatively with histone methyltransferase, suppressor of variegation 3-9 homolog 1 (SUV39H1) and SET domain containing 2 (SETD2) to induce silencing of HBV transcription through modulation of chromatin structure. Our data improved the understanding of histone modifications of the cccDNA minichromosome, thus transcriptional silencing of cccDNA may represent a novel antiviral strategy for the prevention or treatment of HBV infection.Chronic hepatitis B virus (HBV) infection is a significant public health burden worldwide. HBV covalently closed circular DNA (cccDNA) organized as a minichromosome in nucleus is responsible for viral persistence and is the key obstacle for a cure of chronic hepatitis B (CHB). Recent studies suggest cccDNA transcription is epigenetically regulated by histone modifications, especially histone acetylation and methylation. In the present study, we identified transcriptionally active histone succinylation (H3K122succ) as a new histone modification on cccDNA minichromosome by using cccDNA ChIP-Seq approach. Silent mating type information regulation 2 homolog 7 (SIRT7), as an NAD+-dependent histone desuccinylase, could bind to cccDNA through interaction with HBV core protein where it catalyzed histone 3 lysine 122 (H3K122) desuccinylation. Moreover, SIRT7 acts cooperatively with histone methyltransferase, suppressor of variegation 3-9 homolog 1 (SUV39H1) and SET domain containing 2 (SETD2) to induce silencing of HBV transcription through modulation of chromatin structure. Our data improved the understanding of histone modifications of the cccDNA minichromosome, thus transcriptional silencing of cccDNA may represent a novel antiviral strategy for the prevention or treatment of HBV infection.
Chronic hepatitis B virus (HBV) infection is a significant public health burden worldwide. HBV covalently closed circular DNA (cccDNA) organized as a minichromosome in nucleus is responsible for viral persistence and is the key obstacle for a cure of chronic hepatitis B (CHB). Recent studies suggest cccDNA transcription is epigenetically regulated by histone modifications, especially histone acetylation and methylation. In the present study, we identified transcriptionally active histone succinylation (H3K122succ) as a new histone modification on cccDNA minichromosome by using cccDNA ChIP-Seq approach. Silent mating type information regulation 2 homolog 7 (SIRT7), as an NAD+-dependent histone desuccinylase, could bind to cccDNA through interaction with HBV core protein where it catalyzed histone 3 lysine 122 (H3K122) desuccinylation. Moreover, SIRT7 acts cooperatively with histone methyltransferase, suppressor of variegation 3–9 homolog 1 (SUV39H1) and SET domain containing 2 (SETD2) to induce silencing of HBV transcription through modulation of chromatin structure. Our data improved the understanding of histone modifications of the cccDNA minichromosome, thus transcriptional silencing of cccDNA may represent a novel antiviral strategy for the prevention or treatment of HBV infection.
Author Wong, Vincent Kam Wai
Long, Quan-Xin
Hu, Jie-Li
Jiang, Hui
Chen, Wei-Xian
Zhou, Hong-Zhong
Ren, Fang
Law, Betty Yuen Kwan
Huang, Ai-Long
Yu, Hai-Bo
Ren, Ji-Hua
He, Lin
Hu, Zhong-Wen
Xu, Hong-Mei
Cheng, Sheng-Tao
Cai, Xue-Fei
Hu, Yuan
Zhong, Shan
Zhang, Wen-Lu
Chen, Yong
Zhang, Zhen-Zhen
Shi, Xiao-Feng
Chen, Juan
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  givenname: Hong-Mei
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  givenname: Zhen-Zhen
  surname: Zhang
  fullname: Zhang, Zhen-Zhen
  organization: Department of Infectious Diseases, The Children’s Hospital of Chongqing Medical University, Chongqing, China
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  givenname: Jie-Li
  surname: Hu
  fullname: Hu, Jie-Li
  organization: The Key Laboratory of Molecular Biology of Infectious Diseases designated by the Chinese Ministry of Education, Chongqing Medical University, Chongqing, China
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  surname: Cai
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  givenname: Wen-Lu
  surname: Zhang
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  organization: The Key Laboratory of Molecular Biology of Infectious Diseases designated by the Chinese Ministry of Education, Chongqing Medical University, Chongqing, China
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  givenname: Quan-Xin
  surname: Long
  fullname: Long, Quan-Xin
  organization: The Key Laboratory of Molecular Biology of Infectious Diseases designated by the Chinese Ministry of Education, Chongqing Medical University, Chongqing, China
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  givenname: Lin
  surname: He
  fullname: He, Lin
  organization: The Key Laboratory of Molecular Biology of Infectious Diseases designated by the Chinese Ministry of Education, Chongqing Medical University, Chongqing, China
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  givenname: Zhong-Wen
  surname: Hu
  fullname: Hu, Zhong-Wen
  organization: The Key Laboratory of Molecular Biology of Infectious Diseases designated by the Chinese Ministry of Education, Chongqing Medical University, Chongqing, China
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  surname: Zhou
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  organization: The Key Laboratory of Molecular Biology of Infectious Diseases designated by the Chinese Ministry of Education, Chongqing Medical University, Chongqing, China
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  surname: Chen
  fullname: Chen, Juan
  organization: The Key Laboratory of Molecular Biology of Infectious Diseases designated by the Chinese Ministry of Education, Chongqing Medical University, Chongqing, China
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Cites_doi 10.1038/ncomms10734
10.1016/S0960-9822(02)01387-8
10.1001/jama.2018.3795
10.1038/nature12038
10.1073/pnas.1518090112
10.1016/j.jhep.2016.02.009
10.1038/s41467-018-05187-4
10.4196/kjpp.2013.17.6.531
10.1126/science.1243462
10.1016/j.cmet.2014.03.014
10.1080/19491034.2016.1264552
10.1016/j.drup.2010.12.001
10.1038/nature11043
10.1038/nature06268
10.1128/JVI.02861-13
10.1002/hep.29479
10.1053/j.gastro.2006.01.001
10.1016/j.molcel.2013.10.010
10.1016/j.cbpa.2012.10.003
10.1038/srep14806
10.1016/j.cytogfr.2017.11.001
10.1101/gad.1399706
10.1002/hep.29912
10.1111/febs.12346
10.1016/j.jhep.2015.06.023
10.1016/j.molcel.2013.06.001
10.1002/hep.29133
10.1038/nrm3293
10.1158/0008-5472.CAN-17-1912
10.1016/j.advms.2015.09.003
10.1016/j.cmet.2014.08.001
10.1242/jcs.042382
10.1016/j.cellsig.2014.11.026
10.1136/gutjnl-2015-309809
10.3390/v9060156
10.1038/ncomms12235
10.1073/pnas.0908365106
10.1186/s13046-018-0819-y
10.1126/science.1207861
10.1172/JCI58847
10.1016/j.antiviral.2018.07.019
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References Allweiss (2021113011215822700_B3) 2017; 9
Nassal (2021113011215822700_B5) 2015; 64
Kiran (2021113011215822700_B34) 2015; 27
Chen (2021113011215822700_B17) 2013; 52
Caballero (2021113011215822700_B2) 2018; 158
Barber (2021113011215822700_B16) 2012; 487
Kiran (2021113011215822700_B26) 2013; 280
Jiang (2021113011215822700_B9) 2013; 496
Riviere (2021113011215822700_B36) 2015; 63
Vazquez (2021113011215822700_B33) 2017; 8
Yang (2021113011215822700_B13) 2018; 78
Belloni (2021113011215822700_B29) 2009; 106
Pollicino (2021113011215822700_B37) 2006; 130
Daujat (2021113011215822700_B38) 2002; 12
Fukuda (2021113011215822700_B20) 2018; 9
Li (2021113011215822700_B21) 2016; 7
Lucifora (2021113011215822700_B27) 2014; 343
Lucifora (2021113011215822700_B4) 2016; 64
Zhang (2021113011215822700_B28) 2017; 66
Watroba (2021113011215822700_B31) 2016; 61
Ryu (2021113011215822700_B18) 2014; 20
Grob (2021113011215822700_B40) 2009; 122
Belloni (2021113011215822700_B23) 2012; 122
Ford (2021113011215822700_B14) 2006; 20
Olmos (2021113011215822700_B32) 2011; 14
Chen (2021113011215822700_B19) 2016; 7
Tan (2021113011215822700_B10) 2014; 19
Pandey (2021113011215822700_B41) 2015; 5
Tang (2021113011215822700_B1) 2018; 319
Ren (2021113011215822700_B22) 2014; 88
Mendes (2021113011215822700_B30) 2017; 38
Vaquero (2021113011215822700_B39) 2007; 450
Sauve (2021113011215822700_B8) 2012; 16
Du (2021113011215822700_B11) 2011; 334
Li (2021113011215822700_B35) 2018; 37
Ren (2021113011215822700_B25) 2018; 68
Hong (2021113011215822700_B6) 2017; 66
Kim (2021113011215822700_B15) 2013; 64
Tropberger (2021113011215822700_B24) 2015; 112
Park (2021113011215822700_B12) 2013; 50
Houtkooper (2021113011215822700_B7) 2012; 13
References_xml – volume: 7
  start-page: 10734
  year: 2016
  ident: 2021113011215822700_B19
  article-title: SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA processing
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms10734
– volume: 12
  start-page: 2090
  year: 2002
  ident: 2021113011215822700_B38
  article-title: Crosstalk between CARM1 methylation and CBP acetylation on histone H3
  publication-title: Curr. Biol.
  doi: 10.1016/S0960-9822(02)01387-8
– volume: 319
  start-page: 1802
  year: 2018
  ident: 2021113011215822700_B1
  article-title: Chronic hepatitis B infection: a review
  publication-title: JAMA
  doi: 10.1001/jama.2018.3795
– volume: 496
  start-page: 110
  year: 2013
  ident: 2021113011215822700_B9
  article-title: SIRT6 regulates TNF-alpha secretion through hydrolysis of long-chain fatty acyl lysine
  publication-title: Nature
  doi: 10.1038/nature12038
– volume: 112
  start-page: E5715
  year: 2015
  ident: 2021113011215822700_B24
  article-title: Mapping of histone modifications in episomal HBV cccDNA uncovers an unusual chromatin organization amenable to epigenetic manipulation
  publication-title: Proc. Natl. Acad. Sci. U.S.A
  doi: 10.1073/pnas.1518090112
– volume: 64
  start-page: S41
  year: 2016
  ident: 2021113011215822700_B4
  article-title: Attacking hepatitis B virus cccDNA–The holy grail to hepatitis B cure
  publication-title: J. Hepatol.
  doi: 10.1016/j.jhep.2016.02.009
– volume: 9
  start-page: 2833
  year: 2018
  ident: 2021113011215822700_B20
  article-title: SIRT7 has a critical role in bone formation by regulating lysine acylation of SP7/Osterix
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-018-05187-4
– volume: 64
  start-page: 531
  year: 2013
  ident: 2021113011215822700_B15
  article-title: SIRT7 an emerging sirtuin: deciphering newer roles
  publication-title: J. Physiol. Pharmacol.
  doi: 10.4196/kjpp.2013.17.6.531
– volume: 343
  start-page: 1221
  year: 2014
  ident: 2021113011215822700_B27
  article-title: Specific and nonhepatotoxic degradation of nuclear hepatitis B virus cccDNA
  publication-title: Science
  doi: 10.1126/science.1243462
– volume: 19
  start-page: 605
  year: 2014
  ident: 2021113011215822700_B10
  article-title: Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
  publication-title: Cell Metab.
  doi: 10.1016/j.cmet.2014.03.014
– volume: 8
  start-page: 107
  year: 2017
  ident: 2021113011215822700_B33
  article-title: Sirtuins and DNA damage repair: SIRT7 comes to play
  publication-title: Nucleus
  doi: 10.1080/19491034.2016.1264552
– volume: 14
  start-page: 35
  year: 2011
  ident: 2021113011215822700_B32
  article-title: Interplay between SIRT proteins and tumour suppressor transcription factors in chemotherapeutic resistance of cancer
  publication-title: Drug Resist. Updat.
  doi: 10.1016/j.drup.2010.12.001
– volume: 487
  start-page: 114
  year: 2012
  ident: 2021113011215822700_B16
  article-title: SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation
  publication-title: Nature
  doi: 10.1038/nature11043
– volume: 450
  start-page: 440
  year: 2007
  ident: 2021113011215822700_B39
  article-title: SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation
  publication-title: Nature
  doi: 10.1038/nature06268
– volume: 88
  start-page: 2442
  year: 2014
  ident: 2021113011215822700_B22
  article-title: Sirtuin 1 regulates hepatitis B virus transcription and replication by targeting transcription factor AP-1
  publication-title: J. Virol.
  doi: 10.1128/JVI.02861-13
– volume: 66
  start-page: 2066
  year: 2017
  ident: 2021113011215822700_B6
  article-title: Epigenetic regulation of hepatitis B virus covalently closed circular DNA: Implications for epigenetic therapy against chronic hepatitis B
  publication-title: Hepatology
  doi: 10.1002/hep.29479
– volume: 130
  start-page: 823
  year: 2006
  ident: 2021113011215822700_B37
  article-title: Hepatitis B virus replication is regulated by the acetylation status of hepatitis B virus cccDNA-bound H3 and H4 histones
  publication-title: Gastroenterology
  doi: 10.1053/j.gastro.2006.01.001
– volume: 52
  start-page: 303
  year: 2013
  ident: 2021113011215822700_B17
  article-title: Repression of RNA polymerase I upon stress is caused by inhibition of RNA-dependent deacetylation of PAF53 by SIRT7
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2013.10.010
– volume: 16
  start-page: 535
  year: 2012
  ident: 2021113011215822700_B8
  article-title: Sirtuins: NAD(+)-dependent deacetylase mechanism and regulation
  publication-title: Curr. Opin. Chem. Biol.
  doi: 10.1016/j.cbpa.2012.10.003
– volume: 5
  start-page: 14806
  year: 2015
  ident: 2021113011215822700_B41
  article-title: Stabilization of SIRT7 deacetylase by viral oncoprotein HBx leads to inhibition of growth restrictive RPS7 gene and facilitates cellular transformation
  publication-title: Sci. Rep.
  doi: 10.1038/srep14806
– volume: 38
  start-page: 98
  year: 2017
  ident: 2021113011215822700_B30
  article-title: Nuclear sirtuins and inflammatory signaling pathways
  publication-title: Cytokine Growth Factor Rev.
  doi: 10.1016/j.cytogfr.2017.11.001
– volume: 20
  start-page: 1075
  year: 2006
  ident: 2021113011215822700_B14
  article-title: Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
  publication-title: Genes Dev.
  doi: 10.1101/gad.1399706
– volume: 68
  start-page: 1260
  year: 2018
  ident: 2021113011215822700_B25
  article-title: SIRT3 restricts hepatitis B virus transcription and replication through epigenetic regulation of covalently closed circular DNA involving suppressor of variegation 3-9 homolog 1 and SET domain containing 1A histone methyltransferases
  publication-title: Hepatology
  doi: 10.1002/hep.29912
– volume: 280
  start-page: 3451
  year: 2013
  ident: 2021113011215822700_B26
  article-title: Intracellular distribution of human SIRT7 and mapping of the nuclear/nucleolar localization signal
  publication-title: FEBS J.
  doi: 10.1111/febs.12346
– volume: 63
  start-page: 1093
  year: 2015
  ident: 2021113011215822700_B36
  article-title: HBx relieves chromatin-mediated transcriptional repression of hepatitis B viral cccDNA involving SETDB1 histone methyltransferase
  publication-title: J. Hepatol.
  doi: 10.1016/j.jhep.2015.06.023
– volume: 50
  start-page: 919
  year: 2013
  ident: 2021113011215822700_B12
  article-title: SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2013.06.001
– volume: 66
  start-page: 398
  year: 2017
  ident: 2021113011215822700_B28
  article-title: PRMT5 restricts hepatitis B virus replication through epigenetic repression of covalently closed circular DNA transcription and interference with pregenomic RNA encapsidation
  publication-title: Hepatology
  doi: 10.1002/hep.29133
– volume: 13
  start-page: 225
  year: 2012
  ident: 2021113011215822700_B7
  article-title: Sirtuins as regulators of metabolism and healthspan
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/nrm3293
– volume: 78
  start-page: 372
  year: 2018
  ident: 2021113011215822700_B13
  article-title: SHMT2 desuccinylation by SIRT5 drives cancer cell proliferation
  publication-title: Cancer Res.
  doi: 10.1158/0008-5472.CAN-17-1912
– volume: 61
  start-page: 52
  year: 2016
  ident: 2021113011215822700_B31
  article-title: The role of sirtuins in aging and age-related diseases
  publication-title: Adv. Med. Sci.
  doi: 10.1016/j.advms.2015.09.003
– volume: 20
  start-page: 856
  year: 2014
  ident: 2021113011215822700_B18
  article-title: A SIRT7-dependent acetylation switch of GABPbeta1 controls mitochondrial function
  publication-title: Cell Metab.
  doi: 10.1016/j.cmet.2014.08.001
– volume: 122
  start-page: 489
  year: 2009
  ident: 2021113011215822700_B40
  article-title: Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.042382
– volume: 27
  start-page: 673
  year: 2015
  ident: 2021113011215822700_B34
  article-title: Sirtuin 7 in cell proliferation, stress and disease: rise of the seventh Sirtuin!
  publication-title: Cell. Signal.
  doi: 10.1016/j.cellsig.2014.11.026
– volume: 64
  start-page: 1972
  year: 2015
  ident: 2021113011215822700_B5
  article-title: HBV cccDNA: viral persistence reservoir and key obstacle for a cure of chronic hepatitis B
  publication-title: Gut
  doi: 10.1136/gutjnl-2015-309809
– volume: 9
  start-page: 156
  year: 2017
  ident: 2021113011215822700_B3
  article-title: The role of cccDNA in HBV maintenance
  publication-title: Viruses
  doi: 10.3390/v9060156
– volume: 7
  start-page: 12235
  year: 2016
  ident: 2021113011215822700_B21
  article-title: SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms12235
– volume: 106
  start-page: 19975
  year: 2009
  ident: 2021113011215822700_B29
  article-title: Nuclear HBx binds the HBV minichromosome and modifies the epigenetic regulation of cccDNA function
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.0908365106
– volume: 37
  start-page: 148
  year: 2018
  ident: 2021113011215822700_B35
  article-title: SIRT7 suppresses the epithelial-to-mesenchymal transition in oral squamous cell carcinoma metastasis by promoting SMAD4 deacetylation
  publication-title: J. Exp. Clin. Cancer Res.
  doi: 10.1186/s13046-018-0819-y
– volume: 334
  start-page: 806
  year: 2011
  ident: 2021113011215822700_B11
  article-title: Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
  publication-title: Science
  doi: 10.1126/science.1207861
– volume: 122
  start-page: 529
  year: 2012
  ident: 2021113011215822700_B23
  article-title: IFN-alpha inhibits HBV transcription and replication in cell culture and in humanized mice by targeting the epigenetic regulation of the nuclear cccDNA minichromosome
  publication-title: J. Clin. Invest.
  doi: 10.1172/JCI58847
– volume: 158
  start-page: 34
  year: 2018
  ident: 2021113011215822700_B2
  article-title: Hepatitis B virus: the challenge of an ancient virus with multiple faces and a remarkable replication strategy
  publication-title: Antiviral Res.
  doi: 10.1016/j.antiviral.2018.07.019
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Snippet Chronic hepatitis B virus (HBV) infection is a significant public health burden worldwide. HBV covalently closed circular DNA (cccDNA) organized as a...
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Title SIRT7 restricts HBV transcription and replication through catalyzing desuccinylation of histone H3 associated with cccDNA minichromosome
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