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Volumn 85, Issue 21, 2011, Pages 11457-11467

Inhibition of hepatitis B virus replication by cIAP2 involves accelerating the ubiquitin-proteasome-mediated destruction of polymerase

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR INHIBITOR OF APOPTOSIS PROTEIN 2; DNA POLYMERASE; INHIBITOR OF APOPTOSIS PROTEIN 2; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS RNA;

EID: 80055102051     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00879-11     Document Type: Article
Times cited : (21)

References (49)
  • 2
    • 0025026431 scopus 로고
    • The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation
    • Bartenschlager, R., M. Junker-Niepmann, and H. Schaller. 1990. The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation. J. Virol. 64:5324-5332.
    • (1990) J. Virol. , vol.64 , pp. 5324-5332
    • Bartenschlager, R.1    Junker-Niepmann, M.2    Schaller, H.3
  • 3
    • 66949138341 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2
    • Bertrand, M. J., et al. 2009. Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2. Immunity 30:789-801.
    • (2009) Immunity , vol.30 , pp. 789-801
    • Bertrand, M.J.1
  • 4
    • 0037379219 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha inhibition of hepatitis B virus replication involves disruption of capsid integrity through activation of NF-kB
    • Biermer, M., R. Puro, and R. J. Schneider. 2003. Tumor necrosis factor alpha inhibition of hepatitis B virus replication involves disruption of capsid integrity through activation of NF-kB. J. Virol. 77:4033-4042.
    • (2003) J. Virol. , vol.77 , pp. 4033-4042
    • Biermer, M.1    Puro, R.2    Schneider, R.J.3
  • 5
    • 72949113082 scopus 로고    scopus 로고
    • Endolysosomal proteases and their inhibitors in immunity
    • Bird, P. I., J. A. Trapani, and J. A. Villadangos. 2009. Endolysosomal proteases and their inhibitors in immunity. Nat. Rev. Immunol. 9:871-882.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 871-882
    • Bird, P.I.1    Trapani, J.A.2    Villadangos, J.A.3
  • 6
    • 0035861455 scopus 로고    scopus 로고
    • Calcium signaling by HBx protein in hepatitis B virus DNA replication
    • Bouchard, M. J., L. H. Wang, and R. J. Schneider. 2001. Calcium signaling by HBx protein in hepatitis B virus DNA replication. Science 294:2376-2378.
    • (2001) Science , vol.294 , pp. 2376-2378
    • Bouchard, M.J.1    Wang, L.H.2    Schneider, R.J.3
  • 7
    • 7444263584 scopus 로고    scopus 로고
    • Detection and characterization of cytoplasmic hepatitis B virus reverse transcriptase
    • Cao, F., and J. E. Tavis. 2004. Detection and characterization of cytoplasmic hepatitis B virus reverse transcriptase. J. Gen. Virol. 85:3353-3360.
    • (2004) J. Gen. Virol. , vol.85 , pp. 3353-3360
    • Cao, F.1    Tavis, J.E.2
  • 8
    • 78149299837 scopus 로고    scopus 로고
    • Proteasome inhibitors: dozens of molecules and still counting
    • de Bettignies, G., and O. Coux. 2010. Proteasome inhibitors: dozens of molecules and still counting. Biochimie 92:1530-1545.
    • (2010) Biochimie , vol.92 , pp. 1530-1545
    • de Bettignies, G.1    Coux, O.2
  • 9
    • 1242302409 scopus 로고    scopus 로고
    • EASL International Consensus Conference on Hepatitis B. 13-14 September 2002, Geneva, Switzerland. Consensus statement (long version)
    • de Franchis, R., et al. 2003. EASL International Consensus Conference on Hepatitis B. 13-14 September, 2002, Geneva, Switzerland. Consensus statement (long version). J. Hepatol 39(Suppl. 1):S3-S25.
    • (2003) J. Hepatol , vol.39 , Issue.SUPPL. 1
    • de Franchis, R.1
  • 10
    • 0028987482 scopus 로고
    • Mutations in the epsilon sequences of human hepatitis B virus affect both RNA encapsidation and reverse transcription
    • Fallows, D. A., and S. P. Goff. 1995. Mutations in the epsilon sequences of human hepatitis B virus affect both RNA encapsidation and reverse transcription. J. Virol. 69:3067-3073.
    • (1995) J. Virol. , vol.69 , pp. 3067-3073
    • Fallows, D.A.1    Goff, S.P.2
  • 11
    • 0027272786 scopus 로고
    • Translation of the hepatitis B virus P gene by ribosomal scanning as an alternative to internal initiation
    • Fouillot, N., S. Tlouzeau, J. M. Rossignol, and O. Jean-Jean. 1993. Translation of the hepatitis B virus P gene by ribosomal scanning as an alternative to internal initiation. J. Virol. 67:4886-4895.
    • (1993) J. Virol. , vol.67 , pp. 4886-4895
    • Fouillot, N.1    Tlouzeau, S.2    Rossignol, J.M.3    Jean-Jean, O.4
  • 12
    • 34249945560 scopus 로고    scopus 로고
    • Formation of hepatitis B virus covalently closed circular DNA: removal of genome-linked protein
    • Gao, W., and J. Hu. 2007. Formation of hepatitis B virus covalently closed circular DNA: removal of genome-linked protein. J. Virol. 81:6164-6174.
    • (2007) J. Virol. , vol.81 , pp. 6164-6174
    • Gao, W.1    Hu, J.2
  • 13
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman, M. H., and A. Ciechanover. 2002. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82:373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 14
    • 0035062597 scopus 로고    scopus 로고
    • Noncytolytic control of viral infec-tions by the innate and adaptive immune response
    • Guidotti, L. G., and F. V. Chisari. 2001. Noncytolytic control of viral infec-tions by the innate and adaptive immune response. Annu. Rev. Immunol. 19:65-91.
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 65-91
    • Guidotti, L.G.1    Chisari, F.V.2
  • 15
    • 0030021968 scopus 로고    scopus 로고
    • Intracellular inactivation of the hepatitis B virus by cytotoxic T lymphocytes
    • Guidotti, L. G., et al. 1996. Intracellular inactivation of the hepatitis B virus by cytotoxic T lymphocytes. Immunity 4:25-36.
    • (1996) Immunity , vol.4 , pp. 25-36
    • Guidotti, L.G.1
  • 16
    • 0033617583 scopus 로고    scopus 로고
    • Viral clearance without destruction of infected cells during acute HBV infection
    • Guidotti, L. G., et al. 1999. Viral clearance without destruction of infected cells during acute HBV infection. Science 284:825-829.
    • (1999) Science , vol.284 , pp. 825-829
    • Guidotti, L.G.1
  • 17
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding, H. P., Y. Zhang, and D. Ron. 1999. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397:271-274.
    • (1999) Nature , vol.397
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 19
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu, J., and C. Seeger. 1996. Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc. Natl. Acad. Sci. U. S. A. 93:1060-1064.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 20
    • 31044455309 scopus 로고    scopus 로고
    • cIAP2 is a ubiquitin protein ligase for BCL10 and is dysregulated in mucosa-associated lymphoid tissue lymphomas
    • Hu, S., et al. 2006. cIAP2 is a ubiquitin protein ligase for BCL10 and is dysregulated in mucosa-associated lymphoid tissue lymphomas. J. Clin. Invest. 116:174-181.
    • (2006) J. Clin. Invest. , vol.116 , pp. 174-181
    • Hu, S.1
  • 21
    • 0032816238 scopus 로고    scopus 로고
    • Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex
    • Hu, Z., et al. 1999. Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex. J. Virol. 73:7231-7240.
    • (1999) J. Virol. , vol.73 , pp. 7231-7240
    • Hu, Z.1
  • 22
    • 0034282432 scopus 로고    scopus 로고
    • The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7
    • Huang, H., et al. 2000. The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. J. Biol. Chem. 275:26661-26664.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26661-26664
    • Huang, H.1
  • 23
    • 37649020435 scopus 로고    scopus 로고
    • Ubiquitindependent and -independent proteasomal degradation of hepatitis B virus X protein
    • Kim, J. H., S. Y. Sohn, T. S. Benedict Yen, and B. Y. Ahn. 2008. Ubiquitindependent and -independent proteasomal degradation of hepatitis B virus X protein. Biochem. Biophys. Res. Commun. 366:1036-1042.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 1036-1042
    • Kim, J.H.1    Sohn, S.Y.2    Benedict Yen, T.S.3    Ahn, B.Y.4
  • 24
    • 72849142577 scopus 로고    scopus 로고
    • MKRN1 induces degradation of West Nile virus capsid protein by functioning as an E3 ligase
    • Ko, A., et al. 2010. MKRN1 induces degradation of West Nile virus capsid protein by functioning as an E3 ligase. J. Virol. 84:426-436.
    • (2010) J. Virol. , vol.84 , pp. 426-436
    • Ko, A.1
  • 25
    • 0030842540 scopus 로고    scopus 로고
    • Inducible expression of human hepatitis B virus (HBV) in stably transfected hepatoblastoma cells: a novel system for screening potential inhibitors of HBV replication
    • Ladner, S. K., et al. 1997. Inducible expression of human hepatitis B virus (HBV) in stably transfected hepatoblastoma cells: a novel system for screening potential inhibitors of HBV replication. Antimicrob. Agents Chemother. 41:1715-1720.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1715-1720
    • Ladner, S.K.1
  • 26
    • 77953295897 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by MyD88 involves accelerated degradation of pregenomic RNA and nuclear retention of pre-S/S RNAs
    • Li, J., et al. 2010. Inhibition of hepatitis B virus replication by MyD88 involves accelerated degradation of pregenomic RNA and nuclear retention of pre-S/S RNAs. J. Virol. 84:6387-6399.
    • (2010) J. Virol. , vol.84 , pp. 6387-6399
    • Li, J.1
  • 27
    • 49349107931 scopus 로고    scopus 로고
    • Id-1 induces proteasome-dependent degradation of the HBX protein
    • Ling, M. T., et al. 2008. Id-1 induces proteasome-dependent degradation of the HBX protein. J. Mol. Biol. 382:34-43.
    • (2008) J. Mol. Biol. , vol.382 , pp. 34-43
    • Ling, M.T.1
  • 28
    • 27144439034 scopus 로고    scopus 로고
    • Cellular cIAP2 gene expression associated with anti-HBV activity of TNF-α in hepatoblastoma cells
    • Liu, X., et al. 2005. Cellular cIAP2 gene expression associated with anti-HBV activity of TNF-α in hepatoblastoma cells. J. Interferon Cytokine Res. 25: 617-626.
    • (2005) J. Interferon Cytokine Res. , vol.25 , pp. 617-626
    • Liu, X.1
  • 29
    • 50149121101 scopus 로고    scopus 로고
    • Both cIAP1 and cIAP2 regulate TNFα-mediated NF-kB activation
    • Mahoney, D. J., et al. 2008. Both cIAP1 and cIAP2 regulate TNFα-mediated NF-kB activation. Proc. Natl. Acad. Sci. U. S. A. 105:11778-11783.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 11778-11783
    • Mahoney, D.J.1
  • 30
    • 77951247349 scopus 로고    scopus 로고
    • Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-β) and cellular antiviral response
    • Mao, A. P., et al. 2010. Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-β) and cellular antiviral response. J. Biol. Chem. 285:9470-9476.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9470-9476
    • Mao, A.P.1
  • 31
    • 34447260029 scopus 로고    scopus 로고
    • Tumor necrosis factor activates a conserved innate antiviral response to hepatitis B virus that destabilizes nucleocapsids and reduces nuclear viral DNA
    • Puro, R., and R. J. Schneider. 2007. Tumor necrosis factor activates a conserved innate antiviral response to hepatitis B virus that destabilizes nucleocapsids and reduces nuclear viral DNA. J. Virol. 81:7351-7362.
    • (2007) J. Virol. , vol.81 , pp. 7351-7362
    • Puro, R.1    Schneider, R.J.2
  • 33
    • 0036118316 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by interferon requires proteasome activity
    • Robek, M. D., S. F. Wieland, and F. V. Chisari. 2002. Inhibition of hepatitis B virus replication by interferon requires proteasome activity. J. Virol. 76: 3570-3574.
    • (2002) J. Virol. , vol.76 , pp. 3570-3574
    • Robek, M.D.1    Wieland, S.F.2    Chisari, F.V.3
  • 34
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe, M., M. G. Pan, W. J. Henzel, T. M. Ayres, and D. V. Goeddel. 1995. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83:1243-1252.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 35
    • 22144439367 scopus 로고    scopus 로고
    • Type I and type II interferons delay human neutrophil apoptosis via activation of STAT3 and up-regulation of cellular inhibitor of apoptosis 2
    • Sakamoto, E., et al. 2005. Type I and type II interferons delay human neutrophil apoptosis via activation of STAT3 and up-regulation of cellular inhibitor of apoptosis 2. J. Leukoc. Biol. 78:301-309.
    • (2005) J. Leukoc. Biol. , vol.78 , pp. 301-309
    • Sakamoto, E.1
  • 36
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: blocking the road to death's door
    • Salvesen, G. S., and C. S. Duckett. 2002. IAP proteins: blocking the road to death's door. Nat. Rev. Mol. Cell Biol. 3:401-410.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 38
    • 0033230435 scopus 로고    scopus 로고
    • Regulation of translation initiation following stress
    • Sheikh, M. S., and A. J. Fornace, Jr. 1999. Regulation of translation initiation following stress. Oncogene 18:6121-6128.
    • (1999) Oncogene , vol.18 , pp. 6121-6128
    • Sheikh, M.S.1    Fornace Jr., A.J.2
  • 39
    • 33846483634 scopus 로고    scopus 로고
    • E6AP ubiquitin ligase mediates ubiquitylation and degradation of hepatitis C virus core protein
    • Shirakura, M., et al. 2007. E6AP ubiquitin ligase mediates ubiquitylation and degradation of hepatitis C virus core protein. J. Virol. 81:1174-1185.
    • (2007) J. Virol. , vol.81 , pp. 1174-1185
    • Shirakura, M.1
  • 42
    • 22244456417 scopus 로고    scopus 로고
    • Interferon prevents formation of replication-competent hepatitis B virus RNA-containing nucleocapsids
    • Wieland, S. F., A. Eustaquio, C. Whitten-Bauer, B. Boyd, and F. V. Chisari. 2005. Interferon prevents formation of replication-competent hepatitis B virus RNA-containing nucleocapsids. Proc. Natl. Acad. Sci. U. S. A. 102: 9913-9917.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9913-9917
    • Wieland, S.F.1    Eustaquio, A.2    Whitten-Bauer, C.3    Boyd, B.4    Chisari, F.V.5
  • 43
    • 77956037778 scopus 로고    scopus 로고
    • Interferons accelerate decay of replication-competent nucleocapsids of hepatitis B virus
    • Xu, C., et al. 2010. Interferons accelerate decay of replication-competent nucleocapsids of hepatitis B virus. J. Virol. 84:9332-9340.
    • (2010) J. Virol. , vol.84 , pp. 9332-9340
    • Xu, C.1
  • 44
    • 34247476367 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis of trihydrophobin 1 (TH1) by the human papilloma virus E6-associated protein (E6-AP)
    • Yang, Y., et al. 2007. Ubiquitin-dependent proteolysis of trihydrophobin 1 (TH1) by the human papilloma virus E6-associated protein (E6-AP). J. Cell. Biochem. 101:167-180.
    • (2007) J. Cell. Biochem. , vol.101 , pp. 167-180
    • Yang, Y.1
  • 45
    • 77955290279 scopus 로고    scopus 로고
    • Hepatitis B virus polymerase inhibits RIG-I- and Toll-like receptor 3-mediated beta interferon induction in human hepatocytes through interference with interferon regulatory factor 3 activation and dampening of the interaction between TBK1/IKKε and DDX3
    • Yu, S., et al. 2010. Hepatitis B virus polymerase inhibits RIG-I- and Toll-like receptor 3-mediated beta interferon induction in human hepatocytes through interference with interferon regulatory factor 3 activation and dampening of the interaction between TBK1/IKKε and DDX3. J. Gen. Virol. 91:2080-2090.
    • (2010) J. Gen. Virol. , vol.91 , pp. 2080-2090
    • Yu, S.1
  • 46
    • 56349164239 scopus 로고    scopus 로고
    • Noncanonical NF-kB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2. RAF2 and TRAF3 and the kinase NIK
    • Zarnegar, B. J., et al. 2008. Noncanonical NF-kB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK. Nat. Immunol. 9:1371-1378.
    • (2008) TNat. Immunol. , vol.9 , pp. 1371-1378
    • Zarnegar, B.J.1
  • 47
    • 16544364359 scopus 로고    scopus 로고
    • Inhibition of cellular proteasome activities enhances hepadnavirus replication in an HBXdependent manner
    • Zhang, Z., U. Protzer, Z. Hu, J. Jacob, and T. J. Liang. 2004. Inhibition of cellular proteasome activities enhances hepadnavirus replication in an HBXdependent manner. J. Virol. 78:4566-4572.
    • (2004) J. Virol. , vol.78 , pp. 4566-4572
    • Zhang, Z.1    Protzer, U.2    Hu, Z.3    Jacob, J.4    Liang, T.J.5
  • 48
    • 77956042333 scopus 로고    scopus 로고
    • Inhibition of cellular proteasome activities mediates HBX-independent hepatitis B virus replication in vivo
    • Zhang, Z., E. Sun, J. H. Ou, and T. J. Liang. 2010. Inhibition of cellular proteasome activities mediates HBX-independent hepatitis B virus replication in vivo. J. Virol. 84:9326-9331.
    • (2010) J. Virol. , vol.84 , pp. 9326-9331
    • Zhang, Z.1    Sun, E.2    Ou, J.H.3    Liang, T.J.4
  • 49
    • 0034685805 scopus 로고    scopus 로고
    • Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex
    • Zhang, Z., et al. 2000. Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex. J. Biol. Chem. 275:15157-15165.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15157-15165
    • Zhang, Z.1


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