Hepatitis B virus replication

References

• 1. Nassal M, Schaller HHepatitis B virus replication. Trends Microbiol. 1993;1:221–228.[PubMed][Google Scholar]
• 2. Nassal M, Schaller HHepatitis B virus replication--an update. J Viral Hepat. 1996;3:217–226.[PubMed][Google Scholar]
• 3. Nassal MHepatitis B virus replication: novel roles for virus-host interactions. Intervirology. 1999;42:100–116.[PubMed][Google Scholar]
• 4. Nassal M. Macromolecular interactions in hepatitis B virus replication and particle formation. In: Cann AJ, editor. Frontiers in Molecular Biology: DNA virus replication. Oxford: Oxford University Press; 2000. pp. 1–40. [PubMed]
• 5. Ganem D, Schneider R. Hepadnaviridae: The Viruses and Their Replication. In: Knipe DM, Howley PM, editors. Fields Virology. 4th ed. Philadelphia: Lippincott Williams & Wilkins; 2001. pp. 2923–2969. [PubMed]
• 6. Seeger C, Mason WSHepatitis B virus biology. Microbiol Mol Biol Rev. 2000;64:51–68.[Google Scholar]
• 7. Schultz U, Grgacic E, Nassal MDuck hepatitis B virus: an invaluable model system for HBV infection. Adv Virus Res. 2004;63:1–70.[PubMed][Google Scholar]
• 8. Summers J, Mason WSReplication of the genome of a hepatitis B--like virus by reverse transcription of an RNA intermediate. Cell. 1982;29:403–415.[PubMed][Google Scholar]
• 9. Protzer U, Nassal M, Chiang PW, Kirschfink M, Schaller HInterferon gene transfer by a hepatitis B virus vector efficiently suppresses wild-type virus infection. Proc Natl Acad Sci USA. 1999;96:10818–10823.[Google Scholar]
• 10. Sun D, Nassal MStable HepG2- and Huh7-based human hepatoma cell lines for efficient regulated expression of infectious hepatitis B virus. J Hepatol. 2006;45:636–645.[PubMed][Google Scholar]
• 11. Ren S, Nassal MHepatitis B virus (HBV) virion and covalently closed circular DNA formation in primary tupaia hepatocytes and human hepatoma cell lines upon HBV genome transduction with replication-defective adenovirus vectors. J Virol. 2001;75:1104–1116.[Google Scholar]
• 12. Isom HC, Abdelhamed AM, Bilello JP, Miller TGBaculovirus-mediated gene transfer for the study of hepatitis B virus. Methods Mol Med. 2004;96:219–237.[PubMed][Google Scholar]
• 13. Köck J, Schlicht HJAnalysis of the earliest steps of hepadnavirus replication: genome repair after infectious entry into hepatocytes does not depend on viral polymerase activity. J Virol. 1993;67:4867–4874.[Google Scholar]
• 14. Köck J, Nassal M, MacNelly S, Baumert TF, Blum HE, von Weizsäcker FEfficient infection of primary tupaia hepatocytes with purified human and woolly monkey hepatitis B virus. J Virol. 2001;75:5084–5089.[Google Scholar]
• 15. von Weizsäcker F, Köck J, MacNelly S, Ren S, Blum HE, Nassal MThe tupaia model for the study of hepatitis B virus: direct infection and HBV genome transduction of primary tupaia hepatocytes. Methods Mol Med. 2004;96:153–161.[PubMed][Google Scholar]
• 16. Köck J, Baumert TF, Delaney WE, Blum HE, von Weizsäcker FInhibitory effect of adefovir and lamivudine on the initiation of hepatitis B virus infection in primary tupaia hepatocytes. Hepatology. 2003;38:1410–1418.[PubMed][Google Scholar]
• 17. Guidotti LG, Matzke B, Schaller H, Chisari FVHigh-level hepatitis B virus replication in transgenic mice. J Virol. 1995;69:6158–6169.[Google Scholar]
• 18. Raney AK, Eggers CM, Kline EF, Guidotti LG, Pontoglio M, Yaniv M, McLachlan ANuclear covalently closed circular viral genomic DNA in the liver of hepatocyte nuclear factor 1 alpha-null hepatitis B virus transgenic mice. J Virol. 2001;75:2900–2911.[Google Scholar]
• 19. Takehara T, Suzuki T, Ohkawa K, Hosui A, Jinushi M, Miyagi T, Tatsumi T, Kanazawa Y, Hayashi NViral covalently closed circular DNA in a non-transgenic mouse model for chronic hepatitis B virus replication. J Hepatol. 2006;44:267–274.[PubMed][Google Scholar]
• 20. Zhu Y, Yamamoto T, Cullen J, Saputelli J, Aldrich CE, Miller DS, Litwin S, Furman PA, Jilbert AR, Mason WSKinetics of hepadnavirus loss from the liver during inhibition of viral DNA synthesis. J Virol. 2001;75:311–322.[Google Scholar]
• 21. Bock CT, Schwinn S, Locarnini S, Fyfe J, Manns MP, Trautwein C, Zentgraf HStructural organization of the hepatitis B virus minichromosome. J Mol Biol. 2001;307:183–196.[PubMed][Google Scholar]
• 22. Tuttleman JS, Pourcel C, Summers JFormation of the pool of covalently closed circular viral DNA in hepadnavirus-infected cells. Cell. 1986;47:451–460.[PubMed][Google Scholar]
• 23. Wu TT, Coates L, Aldrich CE, Summers J, Mason WSIn hepatocytes infected with duck hepatitis B virus, the template for viral RNA synthesis is amplified by an intracellular pathway. Virology. 1990;175:255–261.[PubMed][Google Scholar]
• 24. Addison WR, Walters KA, Wong WW, Wilson JS, Madej D, Jewell LD, Tyrrell DLHalf-life of the duck hepatitis B virus covalently closed circular DNA pool in vivo following inhibition of viral replication. J Virol. 2002;76:6356–6363.[Google Scholar]
• 25. Ganem D, Prince AMHepatitis B virus infection--natural history and clinical consequences. N Engl J Med. 2004;350:1118–1129.[PubMed][Google Scholar]
• 26. Summers J, Smith PM, Horwich ALHepadnavirus envelope proteins regulate covalently closed circular DNA amplification. J Virol. 1990;64:2819–2824.[Google Scholar]
• 27. Zhang YY, Zhang BH, Theele D, Litwin S, Toll E, Summers JSingle-cell analysis of covalently closed circular DNA copy numbers in a hepadnavirus-infected liver. Proc Natl Acad Sci USA. 2003;100:12372–12377.[Google Scholar]
• 28. Zhang YY, Theele DP, Summers JAge-related differences in amplification of covalently closed circular DNA at early times after duck hepatitis B virus infection of ducks. J Virol. 2005;79:9896–9903.[Google Scholar]
• 29. Le Mire MF, Miller DS, Foster WK, Burrell CJ, Jilbert ARCovalently closed circular DNA is the predominant form of duck hepatitis B virus DNA that persists following transient infection. J Virol. 2005;79:12242–12252.[Google Scholar]
• 30. Zoulim FAntiviral therapy of chronic hepatitis B. Antiviral Res. 2006;71:206–215.[PubMed][Google Scholar]
• 31. Zoulim FEntecavir: a new treatment option for chronic hepatitis B. J Clin Virol. 2006;36:8–12.[PubMed][Google Scholar]
• 32. Terré S, Petit MA, Bréchot CDefective hepatitis B virus particles are generated by packaging and reverse transcription of spliced viral RNAs in vivo. J Virol. 1991;65:5539–5543.[Google Scholar]
• 33. Sommer G, van Bömmel F, Will HGenotype-specific synthesis and secretion of spliced hepatitis B virus genomes in hepatoma cells. Virology. 2000;271:371–381.[PubMed][Google Scholar]
• 34. Obert S, Zachmann-Brand B, Deindl E, Tucker W, Bartenschlager R, Schaller HA splice hepadnavirus RNA that is essential for virus replication. EMBO J. 1996;15:2565–2574.[Google Scholar]
• 35. Loeb DD, Mack AA, Tian RA secondary structure that contains the 5' and 3' splice sites suppresses splicing of duck hepatitis B virus pregenomic RNA. J Virol. 2002;76:10195–10202.[Google Scholar]
• 36. Heise T, Sommer G, Reumann K, Meyer I, Will H, Schaal HThe hepatitis B virus PRE contains a splicing regulatory element. Nucleic Acids Res. 2006;34:353–363.[Google Scholar]
• 37. Sen N, Cao F, Tavis JETranslation of duck hepatitis B virus reverse transcriptase by ribosomal shunting. J Virol. 2004;78:11751–11757.[Google Scholar]
• 38. Nassal M, Junker-Niepmann M, Schaller HTranslational inactivation of RNA function: discrimination against a subset of genomic transcripts during HBV nucleocapsid assembly. Cell. 1990;63:1357–1363.[PubMed][Google Scholar]
• 39. Gnatt AL, Cramer P, Fu J, Bushnell DA, Kornberg RDStructural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science. 2001;292:1876–1882.[PubMed][Google Scholar]
• 40. Nesser NK, Peterson DO, Hawley DKRNA polymerase II subunit Rpb9 is important for transcriptional fidelity in vivo. Proc Natl Acad Sci USA. 2006;103:3268–3273.[Google Scholar]
• 41. Cao F, Tavis JESuppression of mRNA accumulation by the duck hepatitis B virus reverse transcriptase. Virology. 2006;350:475–483.[PubMed][Google Scholar]
• 42. Delelis O, Lehmann-Che J, Saïb AFoamy viruses--a world apart. Curr Opin Microbiol. 2004;7:400–406.[PubMed][Google Scholar]
• 43. Fassati A, Goff SPCharacterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1. J Virol. 2001;75:3626–3635.[Google Scholar]
• 44. Iordanskiy S, Berro R, Altieri M, Kashanchi F, Bukrinsky MIntracytoplasmic maturation of the human immunodeficiency virus type 1 reverse transcription complexes determines their capacity to integrate into chromatin. Retrovirology. 2006;3:4.[Google Scholar]
• 45. Ahlquist PParallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses. Nat Rev Microbiol. 2006;4:371–382.[PubMed][Google Scholar]
• 46. Köck J, Nassal M, Deres K, Blum HE, von Weizsäcker FHepatitis B virus nucleocapsids formed by carboxy-terminally mutated core proteins contain spliced viral genomes but lack full-size DNA. J Virol. 2004;78:13812–13818.[Google Scholar]
• 47. Le Pogam S, Chua PK, Newman M, Shih CExposure of RNA templates and encapsidation of spliced viral RNA are influenced by the arginine-rich domain of human hepatitis B virus core antigen (HBcAg 165-173) J Virol. 2005;79:1871–1887.[Google Scholar]
• 48. Perlman DH, Berg EA, O'connor PB, Costello CE, Hu JReverse transcription-associated dephosphorylation of hepadnavirus nucleocapsids. Proc Natl Acad Sci USA. 2005;102:9020–9025.[Google Scholar]
• 49. Melegari M, Wolf SK, Schneider RJHepatitis B virus DNA replication is coordinated by core protein serine phosphorylation and HBx expression. J Virol. 2005;79:9810–9820.[Google Scholar]
• 50. Roseman AM, Berriman JA, Wynne SA, Butler PJ, Crowther RAA structural model for maturation of the hepatitis B virus core. Proc Natl Acad Sci USA. 2005;102:15821–15826.[Google Scholar]
• 51. Böttcher B, Vogel M, Ploss M, Nassal MHigh plasticity of the hepatitis B virus capsid revealed by conformational stress. J Mol Biol. 2006;356:812–822.[PubMed][Google Scholar]
• 52. Hu J, Toft D, Anselmo D, Wang XIn vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins. J Virol. 2002;76:269–279.[Google Scholar]
• 53. Beck J, Nassal MReconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli. J Virol. 2001;75:7410–7419.[Google Scholar]
• 54. Beck J, Nassal MEfficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein. J Biol Chem. 2003;278:36128–36138.[PubMed][Google Scholar]
• 55. Junker-Niepmann M, Bartenschlager R, Schaller HA short cis-acting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA. EMBO J. 1990;9:3389–3396.[Google Scholar]
• 56. Wang GH, Seeger CNovel mechanism for reverse transcription in hepatitis B viruses. J Virol. 1993;67:6507–6512.[Google Scholar]
• 57. Tavis JE, Perri S, Ganem DHepadnavirus reverse transcription initiates within the stem-loop of the RNA packaging signal and employs a novel strand transfer. J Virol. 1994;68:3536–3543.[Google Scholar]
• 58. Nassal M, Rieger AA bulged region of the hepatitis B virus RNA encapsidation signal contains the replication origin for discontinuous first-strand DNA synthesis. J Virol. 1996;70:2764–2773.[Google Scholar]
• 59. Knaus T, Nassal MThe encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function. Nucleic Acids Res. 1993;21:3967–3975.[Google Scholar]
• 60. Pollack JR, Ganem DAn RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation. J Virol. 1993;67:3254–3263.[Google Scholar]
• 61. Pollack JR, Ganem DSite-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis. J Virol. 1994;68:5579–5587.[Google Scholar]
• 62. Rieger A, Nassal MDistinct requirements for primary sequence in the 5'- and 3'-part of a bulge in the hepatitis B virus RNA encapsidation signal revealed by a combined in vivo selection/in vitro amplification system. Nucleic Acids Res. 1995;23:3909–3915.[Google Scholar]
• 63. Fallows DA, Goff SPMutations in the epsilon sequences of human hepatitis B virus affect both RNA encapsidation and reverse transcription. J Virol. 1995;69:3067–3073.[Google Scholar]
• 64. Laskus T, Rakela J, Persing DHThe stem-loop structure of the cis-encapsidation signal is highly conserved in naturally occurring hepatitis B virus variants. Virology. 1994;200:809–812.[PubMed][Google Scholar]
• 65. Lok AS, Akarca U, Greene SMutations in the pre-core region of hepatitis B virus serve to enhance the stability of the secondary structure of the pre-genome encapsidation signal. Proc Natl Acad Sci USA. 1994;91:4077–4081.[Google Scholar]
• 66. Kramvis A, Kew MCStructure and function of the encapsidation signal of hepadnaviridae. J Viral Hepat. 1998;5:357–367.[PubMed][Google Scholar]
• 67. Guarnieri M, Kim KH, Bang G, Li J, Zhou Y, Tang X, Wands J, Tong SPoint mutations upstream of hepatitis B virus core gene affect DNA replication at the step of core protein expression. J Virol. 2006;80:587–595.[Google Scholar]
• 68. Flodell S, Schleucher J, Cromsigt J, Ippel H, Kidd-Ljunggren K, Wijmenga SThe apical stem-loop of the hepatitis B virus encapsidation signal folds into a stable tri-loop with two underlying pyrimidine bulges. Nucleic Acids Res. 2002;30:4803–4811.[Google Scholar]
• 69. Beck J, Bartos H, Nassal MExperimental confirmation of a hepatitis B virus (HBV) epsilon-like bulge-and-loop structure in avian HBV RNA encapsidation signals. Virology. 1997;227:500–504.[PubMed][Google Scholar]
• 70. Beck J, Nassal MSequence- and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B viruses. J Virol. 1997;71:4971–4980.[Google Scholar]
• 71. Hu K, Beck J, Nassal MSELEX-derived aptamers of the duck hepatitis B virus RNA encapsidation signal distinguish critical and non-critical residues for productive initiation of reverse transcription. Nucleic Acids Res. 2004;32:4377–4389.[Google Scholar]
• 72. Hu J, Boyer MHepatitis B virus reverse transcriptase and epsilon RNA sequences required for specific interaction in vitro. J Virol. 2006;80:2141–2150.[Google Scholar]
• 73. Bartenschlager R, Junker-Niepmann M, Schaller HThe P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation. J Virol. 1990;64:5324–5332.[Google Scholar]
• 74. Calvert J, Summers JTwo regions of an avian hepadnavirus RNA pregenome are required in cis for encapsidation. J Virol. 1994;68:2084–2090.[Google Scholar]
• 75. Ostrow KM, Loeb DDCharacterization of the cis-acting contributions to avian hepadnavirus RNA encapsidation. J Virol. 2002;76:9087–9095.[Google Scholar]
• 76. Ostrow KM, Loeb DDChimeras of duck and heron hepatitis B viruses provide evidence for functional interactions between viral components of pregenomic RNA encapsidation. J Virol. 2004;78:8780–8787.[Google Scholar]
• 77. Rieger A, Nassal MSpecific hepatitis B virus minus-strand DNA synthesis requires only the 5' encapsidation signal and the 3'-proximal direct repeat DR1. J Virol. 1996;70:585–589.[Google Scholar]
• 78. Wang GH, Seeger CThe reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis. Cell. 1992;71:663–670.[PubMed][Google Scholar]
• 79. Jeong JK, Yoon GS, Ryu WSEvidence that the 5'-end cap structure is essential for encapsidation of hepatitis B virus pregenomic RNA. J Virol. 2000;74:5502–5508.[Google Scholar]
• 80. Mangus DA, Evans MC, Jacobson APoly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol. 2003;4:223.[Google Scholar]
• 81. Wagner H, Bauer SAll is not Toll: new pathways in DNA recognition. J Exp Med. 2006;203:265–268.[Google Scholar]
• 82. Meylan E, Tschopp JToll-like receptors and RNA helicases: two parallel ways to trigger antiviral responses. Mol Cell. 2006;22:561–569.[PubMed][Google Scholar]
• 83. Cullen BRTranscription and processing of human microRNA precursors. Mol Cell. 2004;16:861–865.[PubMed][Google Scholar]
• 84. Perri S, Ganem DA host factor that binds near the termini of hepatitis B virus pregenomic RNA. J Virol. 1996;70:6803–6809.[Google Scholar]
• 85. Kreft SG, Nassal MhRUL138, a novel human RNA-binding RING-H2 ubiquitin-protein ligase. J Cell Sci. 2003;116:605–616.[PubMed][Google Scholar]
• 86. Bartenschlager R, Schaller HHepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome. EMBO J. 1992;11:3413–3420.[Google Scholar]
• 87. Yao E, Schaller H, Tavis JEThe duck hepatitis B virus polymerase and core proteins accumulate in different patterns from their common mRNA. Virology. 2003;311:81–88.[PubMed][Google Scholar]
• 88. Yao E, Tavis JEKinetics of synthesis and turnover of the duck hepatitis B virus reverse transcriptase. J Biol Chem. 2003;278:1201–1205.[PubMed][Google Scholar]
• 89. Cao F, Tavis JEDetection and characterization of cytoplasmic hepatitis B virus reverse transcriptase. J Gen Virol. 2004;85:3353–3360.[PubMed][Google Scholar]
• 90. Xiong Y, Eickbush THOrigin and evolution of retroelements based upon their reverse transcriptase sequences. EMBO J. 1990;9:3353–3362.[Google Scholar]
• 91. Radziwill G, Tucker W, Schaller HMutational analysis of the hepatitis B virus P gene product: domain structure and RNase H activity. J Virol. 1990;64:613–620.[Google Scholar]
• 92. Bartenschlager R, Schaller HThe amino-terminal domain of the hepadnaviral P-gene encodes the terminal protein (genome-linked protein) believed to prime reverse transcription. EMBO J. 1988;7:4185–4192.[Google Scholar]
• 93. Weber M, Bronsema V, Bartos H, Bosserhoff A, Bartenschlager R, Schaller HHepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription. J Virol. 1994;68:2994–2999.[Google Scholar]
• 94. Zoulim F, Seeger CReverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase. J Virol. 1994;68:6–13.[Google Scholar]
• 95. Lanford RE, Notvall L, Lee H, Beames BTranscomplementation of nucleotide priming and reverse transcription between independently expressed TP and RT domains of the hepatitis B virus reverse transcriptase. J Virol. 1997;71:2996–3004.[Google Scholar]
• 96. Das K, Xiong X, Yang H, Westland CE, Gibbs CS, Sarafianos SG, Arnold EMolecular modeling and biochemical characterization reveal the mechanism of hepatitis B virus polymerase resistance to lamivudine (3TC) and emtricitabine (FTC) J Virol. 2001;75:4771–4779.[Google Scholar]
• 97. Allen MI, Deslauriers M, Andrews CW, Tipples GA, Walters KA, Tyrrell DL, Brown N, Condreay LD. Identification and characterization of mutations in hepatitis B virus resistant to lamivudine. Lamivudine Clinical Investigation Group. Hepatology. 1998;27:1670–1677.[PubMed]
• 98. Beck J, Vogel M, Nassal MdNTP versus NTP discrimination by phenylalanine 451 in duck hepatitis B virus P protein indicates a common structure of the dNTP-binding pocket with other reverse transcriptases. Nucleic Acids Res. 2002;30:1679–1687.[Google Scholar]
• 99. Ferrer-Orta C, Arias A, Escarmís C, Verdaguer NA comparison of viral RNA-dependent RNA polymerases. Curr Opin Struct Biol. 2006;16:27–34.[PubMed][Google Scholar]
• 100. de Jong RN, van der Vliet PC, Brenkman ABAdenovirus DNA replication: protein priming, jumping back and the role of the DNA binding protein DBP. Curr Top Microbiol Immunol. 2003;272:187–211.[PubMed][Google Scholar]
• 101. Kamtekar S, Berman AJ, Wang J, Lázaro JM, de Vega M, Blanco L, Salas M, Steitz TAThe phi29 DNA polymerase: protein-primer structure suggests a model for the initiation to elongation transition. EMBO J. 2006;25:1335–1343.[Google Scholar]
• 102. Hu J, Anselmo DIn vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90. J Virol. 2000;74:11447–11455.[Google Scholar]
• 103. Beck J, Nassal MIn vitro reconstitution of epsilon-dependent duck hepatitis B virus replication initiation. Methods Mol Med. 2004;95:315–325.[PubMed][Google Scholar]
• 104. Cao F, Badtke MP, Metzger LM, Yao E, Adeyemo B, Gong Y, Tavis JEIdentification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptase. J Virol. 2005;79:10164–10170.[Google Scholar]
• 105. Lanford RE, Kim YH, Lee H, Notvall L, Beames BMapping of the hepatitis B virus reverse transcriptase TP and RT domains by transcomplementation for nucleotide priming and by protein-protein interaction. J Virol. 1999;73:1885–1893.[Google Scholar]
• 106. Chen Y, Varani GProtein families and RNA recognition. FEBS J. 2005;272:2088–2097.[PubMed][Google Scholar]
• 107. Schaaf SG, Beck J, Nassal MA small 2'-OH- and base-dependent recognition element downstream of the initiation site in the RNA encapsidation signal is essential for hepatitis B virus replication initiation. J Biol Chem. 1999;274:37787–37794.[PubMed][Google Scholar]
• 108. Tavis JE, Ganem DEvidence for activation of the hepatitis B virus polymerase by binding of its RNA template. J Virol. 1996;70:5741–5750.[Google Scholar]
• 109. Beck J, Nassal MFormation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template. Mol Cell Biol. 1998;18:6265–6272.[Google Scholar]
• 110. Tavis JE, Massey B, Gong YThe duck hepatitis B virus polymerase is activated by its RNA packaging signal, epsilon. J Virol. 1998;72:5789–5796.[Google Scholar]
• 111. Lanford RE, Notvall L, Beames BNucleotide priming and reverse transcriptase activity of hepatitis B virus polymerase expressed in insect cells. J Virol. 1995;69:4431–4439.[Google Scholar]
• 112. Seifer M, Hamatake R, Bifano M, Standring DNGeneration of replication-competent hepatitis B virus nucleocapsids in insect cells. J Virol. 1998;72:2765–2776.[Google Scholar]
• 113. Hu J, Seeger CHsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc Natl Acad Sci USA. 1996;93:1060–1064.[Google Scholar]
• 114. Tang YC, Chang HC, Roeben A, Wischnewski D, Wischnewski N, Kerner MJ, Hartl FU, Hayer-Hartl MStructural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell. 2006;125:903–914.[PubMed][Google Scholar]
• 115. Hartl FU, Hayer-Hartl MMolecular chaperones in the cytosol: from nascent chain to folded protein. Science. 2002;295:1852–1858.[PubMed][Google Scholar]
• 116. Young JC, Agashe VR, Siegers K, Hartl FUPathways of chaperone-mediated protein folding in the cytosol. Nat Rev Mol Cell Biol. 2004;5:781–791.[PubMed][Google Scholar]
• 117. Mayer MP, Bukau BHsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci. 2005;62:670–684.[Google Scholar]
• 118. Young JC, Moarefi I, Hartl FUHsp90: a specialized but essential protein-folding tool. J Cell Biol. 2001;154:267–273.[Google Scholar]
• 119. Pratt WB, Galigniana MD, Morishima Y, Murphy PJRole of molecular chaperones in steroid receptor action. Essays Biochem. 2004;40:41–58.[PubMed][Google Scholar]
• 120. Hu J, Toft DO, Seeger CHepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO J. 1997;16:59–68.[Google Scholar]
• 121. Guisbert E, Herman C, Lu CZ, Gross CA. A chaperone network controls the heat shock response in E. coli. Genes Dev. 2004;18:2812–2821.
• 122. Takaya A, Matsui M, Tomoyasu T, Kaya M, Yamamoto TThe DnaK chaperone machinery converts the native FlhD2C2 hetero-tetramer into a functional transcriptional regulator of flagellar regulon expression in Salmonella. Mol Microbiol. 2006;59:1327–1340.[PubMed][Google Scholar]
• 123. Hennessy F, Nicoll WS, Zimmermann R, Cheetham ME, Blatch GLNot all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Sci. 2005;14:1697–1709.[Google Scholar]
• 124. Brehmer D, Rüdiger S, Gässler CS, Klostermeier D, Packschies L, Reinstein J, Mayer MP, Bukau BTuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Nat Struct Biol. 2001;8:427–432.[PubMed][Google Scholar]
• 125. Walsh P, Bursać D, Law YC, Cyr D, Lithgow TThe J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep. 2004;5:567–571.[Google Scholar]
• 126. Wang X, Qian X, Guo HC, Hu JHeat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase. J Virol. 2003;77:4471–4480.[Google Scholar]
• 127. Cho G, Suh SW, Jung GHBV polymerase interacts independently with N-terminal and C-terminal fragments of Hsp90beta. Biochem Biophys Res Commun. 2000;274:203–211.[PubMed][Google Scholar]
• 128. Hu J, Flores D, Toft D, Wang X, Nguyen DRequirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J Virol. 2004;78:13122–13131.[Google Scholar]
• 129. Bracher A, Hartl FUHsp90 structure: when two ends meet. Nat Struct Mol Biol. 2006;13:478–480.[PubMed][Google Scholar]
• 130. Pratt WB, Toft DORegulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) 2003;228:111–133.[PubMed][Google Scholar]
• 131. Workman PAltered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol Med. 2004;10:47–51.[PubMed][Google Scholar]
• 132. Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, Fritz LC, Burrows FJA high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature. 2003;425:407–410.[PubMed][Google Scholar]
• 133. Park SG, Jung GHuman hepatitis B virus polymerase interacts with the molecular chaperonin Hsp60. J Virol. 2001;75:6962–6968.[Google Scholar]
• 134. Park SG, Lim SO, Jung GBinding site analysis of human HBV pol for molecular chaperonin, hsp60. Virology. 2002;298:116–123.[PubMed][Google Scholar]
• 135. Park SG, Lee SM, Jung GAntisense oligodeoxynucleotides targeted against molecular chaperonin Hsp60 block human hepatitis B virus replication. J Biol Chem. 2003;278:39851–39857.[PubMed][Google Scholar]
• 136. Kim SS, Shin HJ, Cho YH, Rho HM. Expression of stable hepatitis B viral polymerase associated with GRP94 in E. coli. Arch Virol. 2000;145:1305–1320.[PubMed]
• 137. Wang X, Grammatikakis N, Hu JRole of p50/CDC37 in hepadnavirus assembly and replication. J Biol Chem. 2002;277:24361–24367.[PubMed][Google Scholar]
• 138. Holt SE, Aisner DL, Baur J, Tesmer VM, Dy M, Ouellette M, Trager JB, Morin GB, Toft DO, Shay JW, et al Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev. 1999;13:817–826.[Google Scholar]
• 139. Keppler BR, Grady AT, Jarstfer MBThe biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity. J Biol Chem. 2006;281:19840–19848.[PubMed][Google Scholar]
• 140. Burch AD, Weller SKHerpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus. J Virol. 2005;79:10740–10749.[Google Scholar]
• 141. Kampmueller KM, Miller DJThe cellular chaperone heat shock protein 90 facilitates Flock House virus RNA replication in Drosophila cells. J Virol. 2005;79:6827–6837.[Google Scholar]
• 142. Momose F, Naito T, Yano K, Sugimoto S, Morikawa Y, Nagata KIdentification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis. J Biol Chem. 2002;277:45306–45314.[PubMed][Google Scholar]
• 143. Deng T, Sharps J, Fodor E, Brownlee GGIn vitro assembly of PB2 with a PB1-PA dimer supports a new model of assembly of influenza A virus polymerase subunits into a functional trimeric complex. J Virol. 2005;79:8669–8674.[Google Scholar]
• 144. Liu N, Ji L, Maguire ML, Loeb DDcis-Acting sequences that contribute to the synthesis of relaxed-circular DNA of human hepatitis B virus. J Virol. 2004;78:642–649.[Google Scholar]
• 145. Shin MK, Lee J, Ryu WSA novel cis-acting element facilitates minus-strand DNA synthesis during reverse transcription of the hepatitis B virus genome. J Virol. 2004;78:6252–6262.[Google Scholar]
• 146. Tang H, McLachlan AA pregenomic RNA sequence adjacent to DR1 and complementary to epsilon influences hepatitis B virus replication efficiency. Virology. 2002;303:199–210.[PubMed][Google Scholar]
• 147. Abraham TM, Loeb DDBase pairing between the 5' half of epsilon and a cis-acting sequence, phi, makes a contribution to the synthesis of minus-strand DNA for human hepatitis B virus. J Virol. 2006;80:4380–4387.[Google Scholar]
• 148. Harris RS, Liddament MTRetroviral restriction by APOBEC proteins. Nat Rev Immunol. 2004;4:868–877.[PubMed][Google Scholar]
• 149. Turelli P, Mangeat B, Jost S, Vianin S, Trono DInhibition of hepatitis B virus replication by APOBEC3G. Science. 2004;303:1829.[PubMed][Google Scholar]
• 150. Rösler C, Köck J, Kann M, Malim MH, Blum HE, Baumert TF, von Weizsäcker FAPOBEC-mediated interference with hepadnavirus production. Hepatology. 2005;42:301–309.[PubMed][Google Scholar]
• 151. Bonvin M, Achermann F, Greeve I, Stroka D, Keogh A, Inderbitzin D, Candinas D, Sommer P, Wain-Hobson S, Vartanian JP, et al Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication. Hepatology. 2006;43:1364–1374.[PubMed][Google Scholar]
• 152. Ostrow KM, Loeb DDUnderrepresentation of the 3' region of the capsid pregenomic RNA of duck hepatitis B virus. J Virol. 2004;78:2179–2186.[Google Scholar]
• 153. Loeb DD, Hirsch RC, Ganem DSequence-independent RNA cleavages generate the primers for plus strand DNA synthesis in hepatitis B viruses: implications for other reverse transcribing elements. EMBO J. 1991;10:3533–3540.[Google Scholar]
• 154. Staprans S, Loeb DD, Ganem DMutations affecting hepadnavirus plus-strand DNA synthesis dissociate primer cleavage from translocation and reveal the origin of linear viral DNA. J Virol. 1991;65:1255–1262.[Google Scholar]
• 155. Bill CA, Summers JGenomic DNA double-strand breaks are targets for hepadnaviral DNA integration. Proc Natl Acad Sci USA. 2004;101:11135–11140.[Google Scholar]
• 156. Habig JW, Loeb DDThe conformation of the 3' end of the minus-strand DNA makes multiple contributions to template switches during plus-strand DNA synthesis of duck hepatitis B virus. J Virol. 2003;77:12401–12411.[Google Scholar]
• 157. Havert MB, Loeb DDcis-Acting sequences in addition to donor and acceptor sites are required for template switching during synthesis of plus-strand DNA for duck hepatitis B virus. J Virol. 1997;71:5336–5344.[Google Scholar]
• 158. Havert MB, Ji L, Loeb DDAnalysis of duck hepatitis B virus reverse transcription indicates a common mechanism for the two template switches during plus-strand DNA synthesis. J Virol. 2002;76:2763–2769.[Google Scholar]
• 159. Habig JW, Loeb DDTemplate switches during plus-strand DNA synthesis of duck hepatitis B virus are influenced by the base composition of the minus-strand terminal redundancy. J Virol. 2003;77:12412–12420.[Google Scholar]
• 160. Liu N, Tian R, Loeb DDBase pairing among three cis-acting sequences contributes to template switching during hepadnavirus reverse transcription. Proc Natl Acad Sci USA. 2003;100:1984–1989.[Google Scholar]
• 161. Mueller-Hill K, Loeb DDcis-Acting sequences 5E, M, and 3E interact to contribute to primer translocation and circularization during reverse transcription of avian hepadnavirus DNA. J Virol. 2002;76:4260–4266.[Google Scholar]
• 162. Lee J, Shin MK, Lee HJ, Yoon G, Ryu WSThree novel cis-acting elements required for efficient plus-strand DNA synthesis of the hepatitis B virus genome. J Virol. 2004;78:7455–7464.[Google Scholar]
• 163. Wynne SA, Crowther RA, Leslie AGThe crystal structure of the human hepatitis B virus capsid. Mol Cell. 1999;3:771–780.[PubMed][Google Scholar]