메뉴 건너뛰기




Volumn 13, Issue 1, 2007, Pages 91-103

Avian hepatitis B viruses: Molecular and cellular biology, phylogenesis, and host tropism

Author keywords

cccDNA; Endocytosis; Evolution; Fusion; Gene expression; Genome; Hepadnavirus; Hepatocellular differentiation; Host range; In vitro and in vivo infection; Morphogenesis and secretion; Pararetroviruses; Structure; Subviral particela; Transport; Virions

Indexed keywords

DNA VACCINE; DOUBLE STRANDED DNA; ENTECAVIR; INTERFERON; NUCLEOSIDE ANALOG; VIRUS DNA; VIRUS RNA;

EID: 33846555276     PISSN: 10079327     EISSN: None     Source Type: Journal    
DOI: 10.3748/wjg.v13.i1.91     Document Type: Review
Times cited : (52)

References (101)
  • 2
    • 0019949367 scopus 로고
    • Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate
    • Summers J, Mason WS. Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate. Cell 1982; 29: 403-415
    • (1982) Cell , vol.29 , pp. 403-415
    • Summers, J.1    Mason, W.S.2
  • 3
    • 0023028191 scopus 로고
    • Formation of the pool of covalently closed circular viral DNA in hepadnavirus-infected cells
    • Tuttleman JS, Pourcel C, Summers J. Formation of the pool of covalently closed circular viral DNA in hepadnavirus-infected cells. Cell 1986; 47: 451-460
    • (1986) Cell , vol.47 , pp. 451-460
    • Tuttleman, J.S.1    Pourcel, C.2    Summers, J.3
  • 4
    • 0026493753 scopus 로고
    • The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis
    • Wang GH, Seeger C. The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis. Cell 1992; 71: 663-670
    • (1992) Cell , vol.71 , pp. 663-670
    • Wang, G.H.1    Seeger, C.2
  • 5
    • 0029078314 scopus 로고
    • The pre-S domain of the large viral envelope protein determines host range in avian hepatitis B viruses
    • Ishikawa T, Ganem D. The pre-S domain of the large viral envelope protein determines host range in avian hepatitis B viruses. Proc Natl Acad Sci USA 1995; 92: 6259-6263
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6259-6263
    • Ishikawa, T.1    Ganem, D.2
  • 6
    • 0025314572 scopus 로고
    • Efficient duck hepatitis B virus production by an avian liver tumor cell line
    • Condreay LD, Aldrich CE, Coates L, Mason WS, Wu TT. Efficient duck hepatitis B virus production by an avian liver tumor cell line. J Virol 1990; 64: 3249-3258
    • (1990) J Virol , vol.64 , pp. 3249-3258
    • Condreay, L.D.1    Aldrich, C.E.2    Coates, L.3    Mason, W.S.4    Wu, T.T.5
  • 7
    • 0001435504 scopus 로고    scopus 로고
    • Hepadnaviridae: The viruses and their replication
    • In: Knipe DM, Howley PM, eds. Philadelphia: Lippincott, Williams & Wilkins
    • Ganem D, Schneider RJ. Hepadnaviridae: The viruses and their replication. In: Knipe DM, Howley PM, eds. Fields Virology. Volume 2. Philadelphia: Lippincott, Williams & Wilkins, 2001; 2923-2969
    • (2001) Fields Virology , vol.2 , pp. 2923-2969
    • Ganem, D.1    Schneider, R.J.2
  • 8
    • 0019133611 scopus 로고
    • Virus of Pekin ducks with structural and biological relatedness to human hepatitis B virus
    • Mason WS, Seal G, Summers J. Virus of Pekin ducks with structural and biological relatedness to human hepatitis B virus. J Virol 1980; 36: 829-836
    • (1980) J Virol , vol.36 , pp. 829-836
    • Mason, W.S.1    Seal, G.2    Summers, J.3
  • 9
    • 0028421327 scopus 로고
    • Characterisation of the Indian strain of duck hepatitis B virus (DHBV) and development of a carrier duck colony for antiviral drug testing
    • Munshi A, Mehrotra R, Panda SK. Characterisation of the Indian strain of duck hepatitis B virus (DHBV) and development of a carrier duck colony for antiviral drug testing. Trop Gastroenterol 1994; 15: 77-85
    • (1994) Trop Gastroenterol , vol.15 , pp. 77-85
    • Munshi, A.1    Mehrotra, R.2    Panda, S.K.3
  • 10
    • 0035144177 scopus 로고    scopus 로고
    • Sequence comparison of an Australian duck hepatitis B virus strain with other avian hepadnaviruses
    • Triyatni M, Ey P, Tran T, Le Mire M, Qiao M, Burrell C, Jilbert A. Sequence comparison of an Australian duck hepatitis B virus strain with other avian hepadnaviruses. J Gen Virol 2001; 82: 373-378
    • (2001) J Gen Virol , vol.82 , pp. 373-378
    • Triyatni, M.1    Ey, P.2    Tran, T.3    Le Mire, M.4    Qiao, M.5    Burrell, C.6    Jilbert, A.7
  • 12
    • 0033568298 scopus 로고    scopus 로고
    • A new avian hepadnavirus infecting snow geese (Anser caerulescens) produces a significant fraction of virions containing single-stranded DNA
    • Chang SF, Netter HJ, Bruns M, Schneider R, Frolich K, Will H. A new avian hepadnavirus infecting snow geese (Anser caerulescens) produces a significant fraction of virions containing single-stranded DNA. Virology 1999; 262:39-54
    • (1999) Virology , vol.262 , pp. 39-54
    • Chang, S.F.1    Netter, H.J.2    Bruns, M.3    Schneider, R.4    Frolich, K.5    Will, H.6
  • 15
    • 0023803399 scopus 로고
    • Isolation and characterization of a hepatitis B virus endemic in herons
    • Sprengel R, Kaleta EF, Will H. Isolation and characterization of a hepatitis B virus endemic in herons. J Virol 1988; 62: 3832-3839
    • (1988) J Virol , vol.62 , pp. 3832-3839
    • Sprengel, R.1    Kaleta, E.F.2    Will, H.3
  • 16
    • 0028345733 scopus 로고
    • Duck hepatitis B virus infection of Muscovy duck hepatocytes and nature of virus resistance in vivo
    • Pugh JC, Simmons H. Duck hepatitis B virus infection of Muscovy duck hepatocytes and nature of virus resistance in vivo. J Virol 1994; 68: 2487-2494
    • (1994) J Virol , vol.68 , pp. 2487-2494
    • Pugh, J.C.1    Simmons, H.2
  • 18
    • 0023516826 scopus 로고
    • Initiation and termination of duck hepatitis B virus DNA synthesis during virus maturation
    • Lien JM, Petcu DJ, Aldrich CE, Mason WS. Initiation and termination of duck hepatitis B virus DNA synthesis during virus maturation. J Virol 1987; 61:3832-3840
    • (1987) J Virol , vol.61 , pp. 3832-3840
    • Lien, J.M.1    Petcu, D.J.2    Aldrich, C.E.3    Mason, W.S.4
  • 19
    • 0018937889 scopus 로고
    • Hepatitis B virus contains protein attached to the 5′ terminus of its complete DNA strand
    • Gerlich WH, Robinson WS. Hepatitis B virus contains protein attached to the 5′ terminus of its complete DNA strand. Cell 1980; 21: 801-809
    • (1980) Cell , vol.21 , pp. 801-809
    • Gerlich, W.H.1    Robinson, W.S.2
  • 20
    • 0017756176 scopus 로고
    • Structure of hepatitis B Dane particle DNA and nature of the endogenous DNA polymerase reaction
    • Landers TA, Greenberg HB, Robinson WS. Structure of hepatitis B Dane particle DNA and nature of the endogenous DNA polymerase reaction. J Virol 1977; 23: 368-376
    • (1977) J Virol , vol.23 , pp. 368-376
    • Landers, T.A.1    Greenberg, H.B.2    Robinson, W.S.3
  • 21
    • 0022502287 scopus 로고
    • Biochemical and genetic evidence for the hepatitis B virus replication strategy
    • Seeger C, Ganem D, Varmus HE. Biochemical and genetic evidence for the hepatitis B virus replication strategy. Science 1986; 232: 477-484
    • (1986) Science , vol.232 , pp. 477-484
    • Seeger, C.1    Ganem, D.2    Varmus, H.E.3
  • 23
    • 0021865385 scopus 로고
    • Sequence of events in natural infection of Pekin duck embryos with duck hepatitis B virus
    • Urban MK, O'Connell AP, London WT. Sequence of events in natural infection of Pekin duck embryos with duck hepatitis B virus. J Virol 1985; 55: 16-22
    • (1985) J Virol , vol.55 , pp. 16-22
    • Urban, M.K.1    O'Connell, A.P.2    London, W.T.3
  • 24
    • 0020265940 scopus 로고
    • Structure of hepatitis B surface antigen. Characterization of the lipid components and their association with the viral proteins
    • Gavilanes F, Gonzalez-Ros JM, Peterson DL. Structure of hepatitis B surface antigen. Characterization of the lipid components and their association with the viral proteins. J Biol Chem 1982; 257: 7770-7777
    • (1982) J Biol Chem , vol.257 , pp. 7770-7777
    • Gavilanes, F.1    Gonzalez-Ros, J.M.2    Peterson, D.L.3
  • 25
    • 0028809141 scopus 로고
    • Characterization of the HBsAg particle lipid membrane
    • Sonveaux N, Thines D, Ruysschaert JM. Characterization of the HBsAg particle lipid membrane. Res Virol 1995; 146: 43-51
    • (1995) Res Virol , vol.146 , pp. 43-51
    • Sonveaux, N.1    Thines, D.2    Ruysschaert, J.M.3
  • 27
    • 3242688755 scopus 로고    scopus 로고
    • Itinerary of hepatitis B viruses: Delineation of restriction points critical for infectious entry
    • Funk A, Mhamdi M, Lin L, Will H, Sirma H. Itinerary of hepatitis B viruses: delineation of restriction points critical for infectious entry. J Virol 2004; 78: 8289-8300
    • (2004) J Virol , vol.78 , pp. 8289-8300
    • Funk, A.1    Mhamdi, M.2    Lin, L.3    Will, H.4    Sirma, H.5
  • 28
    • 0027430748 scopus 로고
    • Hepadnavirus infection requires interaction between the viral pre-S domain and a specific hepatocellular receptor
    • Klingmuller U, Schaller H. Hepadnavirus infection requires interaction between the viral pre-S domain and a specific hepatocellular receptor. J Virol 1993; 67: 7414-7422
    • (1993) J Virol , vol.67 , pp. 7414-7422
    • Klingmuller, U.1    Schaller, H.2
  • 29
    • 0031883263 scopus 로고    scopus 로고
    • Enhancement of hepatitis B virus infection by noninfectious subviral particles
    • Bruns M, Miska S, Chassot S, Will H. Enhancement of hepatitis B virus infection by noninfectious subviral particles. J Virol 1998; 72: 1462-1468
    • (1998) J Virol , vol.72 , pp. 1462-1468
    • Bruns, M.1    Miska, S.2    Chassot, S.3    Will, H.4
  • 30
    • 0027201547 scopus 로고
    • Hepatitis B virus replication
    • Nassal M, Schaller H. Hepatitis B virus replication. Trends Microbiol 1993; 1: 221-228
    • (1993) Trends Microbiol , vol.1 , pp. 221-228
    • Nassal, M.1    Schaller, H.2
  • 31
    • 0009638796 scopus 로고    scopus 로고
    • Zelluläre Funktionen während der frühen und späten Schritte im Infektionszyklus des Enten Hepatitis B Virus
    • Dissertation der Naturwissenschaftlich-Mathematischen Gesamtfakultät der Ruprecht-Karls-Universität Heidelberg
    • Hildt M. Zelluläre Funktionen während der frühen und späten Schritte im Infektionszyklus des Enten Hepatitis B Virus. Dissertation der Naturwissenschaftlich-Mathematischen Gesamtfakultät der Ruprecht-Karls-Universität Heidelberg, 1996
    • (1996)
    • Hildt, M.1
  • 33
    • 0029793619 scopus 로고    scopus 로고
    • Uptake of duck hepatitis B virus into hepatocytes occurs by endocytosis but does not require passage of the virus through an acidic intracellular compartment
    • Kock J, Borst EM, Schlicht HJ. Uptake of duck hepatitis B virus into hepatocytes occurs by endocytosis but does not require passage of the virus through an acidic intracellular compartment. J Virol 1996; 70: 5827-5831
    • (1996) J Virol , vol.70 , pp. 5827-5831
    • Kock, J.1    Borst, E.M.2    Schlicht, H.J.3
  • 34
    • 33748944981 scopus 로고    scopus 로고
    • pH-independent entry and sequential endosomal sorting are major determinants of hepadnaviral infection in primary hepatocytes
    • Funk A, Mhamdi M, Hohenberg H, Will H, Sirma H. pH-independent entry and sequential endosomal sorting are major determinants of hepadnaviral infection in primary hepatocytes Hepatology 2006; 44: 685-693
    • (2006) Hepatology , vol.44 , pp. 685-693
    • Funk, A.1    Mhamdi, M.2    Hohenberg, H.3    Will, H.4    Sirma, H.5
  • 35
    • 0033526096 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex
    • Kann M, Sodeik B, Vlachou A, Gerlich WH, Helenius A. Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex. J Cell Biol 1999; 145: 45-55
    • (1999) J Cell Biol , vol.145 , pp. 45-55
    • Kann, M.1    Sodeik, B.2    Vlachou, A.3    Gerlich, W.H.4    Helenius, A.5
  • 36
    • 0029037074 scopus 로고
    • The covalently closed duplex form of the hepadnavirus genome exists in situ as a heterogeneous population of viral minichromosomes
    • Newbold JE, Xin H, Tencza M, Sherman G, Dean J, Bowden S, Locarnini S. The covalently closed duplex form of the hepadnavirus genome exists in situ as a heterogeneous population of viral minichromosomes. J Virol 1995; 69: 3350-3357
    • (1995) J Virol , vol.69 , pp. 3350-3357
    • Newbold, J.E.1    Xin, H.2    Tencza, M.3    Sherman, G.4    Dean, J.5    Bowden, S.6    Locarnini, S.7
  • 37
  • 38
    • 0026483273 scopus 로고
    • Hepatitis B virus capsid particles are assembled from core-protein dimer precursors
    • Zhou S, Standring DN. Hepatitis B virus capsid particles are assembled from core-protein dimer precursors. Proc Natl Acad Sci USA 1992; 89: 10046-10050
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10046-10050
    • Zhou, S.1    Standring, D.N.2
  • 39
    • 0033999564 scopus 로고    scopus 로고
    • Core protein phosphorylation modulates pregenomic RNA encapsidation to different extents in human and duck hepatitis B viruses
    • Gazina EV, Fielding JE, Lin B, Anderson DA. Core protein phosphorylation modulates pregenomic RNA encapsidation to different extents in human and duck hepatitis B viruses. J Virol 2000; 74: 4721-4728
    • (2000) J Virol , vol.74 , pp. 4721-4728
    • Gazina, E.V.1    Fielding, J.E.2    Lin, B.3    Anderson, D.A.4
  • 40
    • 0024635927 scopus 로고
    • Characterization of the major duck hepatitis B virus core particle protein
    • Pugh J, Zweidler A, Summers J. Characterization of the major duck hepatitis B virus core particle protein. J Virol 1989; 63: 1371-1376
    • (1989) J Virol , vol.63 , pp. 1371-1376
    • Pugh, J.1    Zweidler, A.2    Summers, J.3
  • 41
    • 0142027756 scopus 로고    scopus 로고
    • Single-cell analysis of covalently closed circular DNA copy numbers in a hepadnavirus-infected liver
    • Zhang YY, Zhang BH, Theele D, Litwin S, Toll E, Summers J. Single-cell analysis of covalently closed circular DNA copy numbers in a hepadnavirus-infected liver. Proc Natl Acad Sci USA 2003; 100: 12372-12377
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12372-12377
    • Zhang, Y.Y.1    Zhang, B.H.2    Theele, D.3    Litwin, S.4    Toll, E.5    Summers, J.6
  • 42
    • 0028334395 scopus 로고
    • Coordinate regulation of replication and virus assembly by the large envelope protein of an avian hepadnavirus
    • Lenhoff RJ, Summers J. Coordinate regulation of replication and virus assembly by the large envelope protein of an avian hepadnavirus. J Virol 1994; 68: 4565-4571
    • (1994) J Virol , vol.68 , pp. 4565-4571
    • Lenhoff, R.J.1    Summers, J.2
  • 44
    • 0026695732 scopus 로고
    • The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly
    • Nassal M. The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly. J Virol 1992; 66: 4107-4116
    • (1992) J Virol , vol.66 , pp. 4107-4116
    • Nassal, M.1
  • 45
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Bottcher B, Wynne SA, Crowther RA. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 1997; 386: 88-91
    • (1997) Nature , vol.386 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 46
    • 0025773026 scopus 로고
    • A domain of the hepadnavirus capsid protein is specifically required for DNA maturation and virus assembly
    • Yu M, Summers J. A domain of the hepadnavirus capsid protein is specifically required for DNA maturation and virus assembly. J Virol 1991; 65: 2511-2517
    • (1991) J Virol , vol.65 , pp. 2511-2517
    • Yu, M.1    Summers, J.2
  • 47
    • 0035132753 scopus 로고    scopus 로고
    • Signals for bidirectional nucleocytoplasmic transport in the duck hepatitis B virus capsid protein
    • Mabit H, Breiner KM, Knaust A, Zachmann-Brand B, Schaller H. Signals for bidirectional nucleocytoplasmic transport in the duck hepatitis B virus capsid protein. J Virol 2001; 75: 1968-1977
    • (2001) J Virol , vol.75 , pp. 1968-1977
    • Mabit, H.1    Breiner, K.M.2    Knaust, A.3    Zachmann-Brand, B.4    Schaller, H.5
  • 48
    • 0028358552 scopus 로고
    • Multiple functions of capsid protein phosphorylation in duck hepatitis B virus replication
    • Yu M, Summers J. Multiple functions of capsid protein phosphorylation in duck hepatitis B virus replication. J Virol 1994; 68: 4341-4348
    • (1994) J Virol , vol.68 , pp. 4341-4348
    • Yu, M.1    Summers, J.2
  • 49
    • 0027167557 scopus 로고
    • An RNA stem-loop structure directs hepatitis B virus genonmic RNA encapsidation
    • Pollack JR, Ganem D. An RNA stem-loop structure directs hepatitis B virus genonmic RNA encapsidation. J Virol 1993; 67: 3254-3263
    • (1993) J Virol , vol.67 , pp. 3254-3263
    • Pollack, J.R.1    Ganem, D.2
  • 50
    • 0005857894 scopus 로고
    • A signal peptide encoded within the precore region of hepatitis B virus directs the secretion of a heterogeneous population of e antigens in Xenopus oocytes
    • Standring DN, Ou JH, Masiarz FR, Rutter WJ. A signal peptide encoded within the precore region of hepatitis B virus directs the secretion of a heterogeneous population of e antigens in Xenopus oocytes. Proc Natl Acad Sci USA 1988; 85: 8405-8409
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8405-8409
    • Standring, D.N.1    Ou, J.H.2    Masiarz, F.R.3    Rutter, W.J.4
  • 51
    • 0023943302 scopus 로고
    • Targeting of the hepatitis B virus precore protein to the endoplasmic reticulum membrane: After signal peptide cleavage translocation can be aborted and the product released into the cytoplasm
    • Garcia PD, Ou JH, Rutter WJ, Walter P. Targeting of the hepatitis B virus precore protein to the endoplasmic reticulum membrane: after signal peptide cleavage translocation can be aborted and the product released into the cytoplasm. J Cell Biol 1988; 106: 1093-1104
    • (1988) J Cell Biol , vol.106 , pp. 1093-1104
    • Garcia, P.D.1    Ou, J.H.2    Rutter, W.J.3    Walter, P.4
  • 52
    • 0023485869 scopus 로고
    • The duck hepatitis B virus pre-C region encodes a signal sequence which is essential for synthesis and secretion of processed core proteins but not for virus formation
    • Schlicht HJ, Salfeld J, Schaller H. The duck hepatitis B virus pre-C region encodes a signal sequence which is essential for synthesis and secretion of processed core proteins but not for virus formation. J Virol 1987; 61: 3701-3709
    • (1987) J Virol , vol.61 , pp. 3701-3709
    • Schlicht, H.J.1    Salfeld, J.2    Schaller, H.3
  • 53
    • 0025877802 scopus 로고
    • Mechanism, kinetics, and role of duck hepatitis B virus e-antigen expression in vivo
    • Schneider R, Fernholz D, Wildner G, Will H. Mechanism, kinetics, and role of duck hepatitis B virus e-antigen expression in vivo. Virology 1991; 182: 503-512
    • (1991) Virology , vol.182 , pp. 503-512
    • Schneider, R.1    Fernholz, D.2    Wildner, G.3    Will, H.4
  • 54
    • 0142151773 scopus 로고    scopus 로고
    • Exploring the biological basis of hepatitis B e antigen in hepatitis B virus infection
    • Milich D, Liang TJ. Exploring the biological basis of hepatitis B e antigen in hepatitis B virus infection. Hepatology 2003; 38: 1075-1086
    • (2003) Hepatology , vol.38 , pp. 1075-1086
    • Milich, D.1    Liang, T.J.2
  • 55
    • 0032954606 scopus 로고    scopus 로고
    • Enrichment of a precore-minus mutant of duck hepatitis B virus in experimental mixed infections
    • Zhang YY, Summers J. Enrichment of a precore-minus mutant of duck hepatitis B virus in experimental mixed infections. J Virol 1999; 73: 3616-3622
    • (1999) J Virol , vol.73 , pp. 3616-3622
    • Zhang, Y.Y.1    Summers, J.2
  • 57
    • 0025061039 scopus 로고
    • Mutational analysis of the hepatitis B virus P gene product: Domain structure and RNase H activity
    • Radziwill G, Tucker W, Schaller H. Mutational analysis of the hepatitis B virus P gene product: domain structure and RNase H activity. J Viral 1990; 64: 613-620
    • (1990) J Viral , vol.64 , pp. 613-620
    • Radziwill, G.1    Tucker, W.2    Schaller, H.3
  • 58
    • 0025076858 scopus 로고
    • Effects of insertional and point mutations on the functions of the duck hepatitis B virus polymerase
    • Chang LJ, Hirsch RC, Ganem D, Varmus HE. Effects of insertional and point mutations on the functions of the duck hepatitis B virus polymerase. J Virol 1990; 64: 5553-5558
    • (1990) J Virol , vol.64 , pp. 5553-5558
    • Chang, L.J.1    Hirsch, R.C.2    Ganem, D.3    Varmus, H.E.4
  • 59
    • 8644249753 scopus 로고    scopus 로고
    • Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function
    • Hu J, Flores D, Toft D, Wang X, Nguyen D. Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J Virol 2004; 78: 13122-13131
    • (2004) J Virol , vol.78 , pp. 13122-13131
    • Hu, J.1    Flores, D.2    Toft, D.3    Wang, X.4    Nguyen, D.5
  • 60
    • 0028300388 scopus 로고
    • Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription
    • Weber M, Bronsema V, Bartos H, Bosserhoff A, Bartenschlager R, Schaller H. Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription. J Virol 1994; 68: 2994-2999
    • (1994) J Virol , vol.68 , pp. 2994-2999
    • Weber, M.1    Bronsema, V.2    Bartos, H.3    Bosserhoff, A.4    Bartenschlager, R.5    Schaller, H.6
  • 61
    • 0029010766 scopus 로고
    • RNA sequences controlling the initiation and transfer of duck hepatitis B virus minus-strand DNA
    • Tavis JE, Ganem D. RNA sequences controlling the initiation and transfer of duck hepatitis B virus minus-strand DNA. J Virol 1995; 69: 4283-4291
    • (1995) J Virol , vol.69 , pp. 4283-4291
    • Tavis, J.E.1    Ganem, D.2
  • 62
    • 0029833252 scopus 로고    scopus 로고
    • Evidence for activation of the hepatitis B virus polymerase by binding of its RNA template
    • Tavis JE, Ganem D. Evidence for activation of the hepatitis B virus polymerase by binding of its RNA template. J Virol 1996; 70: 5741-5750
    • (1996) J Virol , vol.70 , pp. 5741-5750
    • Tavis, J.E.1    Ganem, D.2
  • 64
    • 0022639461 scopus 로고
    • Evidence that a capped oligoribonucleotide is the primer for duck hepatitis B virus plus-strand DNA synthesis
    • Lien JM, Aldrich CE, Mason WS. Evidence that a capped oligoribonucleotide is the primer for duck hepatitis B virus plus-strand DNA synthesis. J Virol 1986; 37: 229-236
    • (1986) J Virol , vol.37 , pp. 229-236
    • Lien, J.M.1    Aldrich, C.E.2    Mason, W.S.3
  • 65
    • 0026033997 scopus 로고
    • Mutations affecting hepadnavirus plus-strand DNA synthesis dissociate primer cleavage from translocation and reveal the origin of linear viral DNA
    • Staprans S, Loeb DD, Ganem D. Mutations 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
    • (1991) J Virol , vol.65 , pp. 1255-1262
    • Staprans, S.1    Loeb, D.D.2    Ganem, D.3
  • 66
    • 0023233802 scopus 로고
    • Characterization of a pre-S polypeptide on the surfaces of infectious avian hepadnavirus particles
    • Pugh JC, Sninsky JJ, Summers JW, Schaeffer E. Characterization of a pre-S polypeptide on the surfaces of infectious avian hepadnavirus particles. J Virol 1987; 61:1384-1390
    • (1987) J Virol , vol.61 , pp. 1384-1390
    • Pugh, J.C.1    Sninsky, J.J.2    Summers, J.W.3    Schaeffer, E.4
  • 67
    • 0023194213 scopus 로고
    • Biochemical and immunological characterization of the duck hepatitis B virus envelope proteins
    • Schlicht HJ, Kuhn C, Guhr B, Mattaliano RJ, Schaller H. Biochemical and immunological characterization of the duck hepatitis B virus envelope proteins. J Virol 1987; 61: 2280-2285
    • (1987) J Virol , vol.61 , pp. 2280-2285
    • Schlicht, H.J.1    Kuhn, C.2    Guhr, B.3    Mattaliano, R.J.4    Schaller, H.5
  • 68
    • 0029848672 scopus 로고    scopus 로고
    • Functions of the large hepatitis B virus surface protein in viral particle morphogenesis
    • Bruss V, Gerhardt E, Vieluf K, Wunderlich G. Functions of the large hepatitis B virus surface protein in viral particle morphogenesis. Intervirology 1996; 39: 23-31
    • (1996) Intervirology , vol.39 , pp. 23-31
    • Bruss, V.1    Gerhardt, E.2    Vieluf, K.3    Wunderlich, G.4
  • 69
    • 0026013628 scopus 로고
    • Myristylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly
    • Macrae DR, Bruss V, Ganem D. Myristylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly. Virology 1991; 181: 359-363
    • (1991) Virology , vol.181 , pp. 359-363
    • Macrae, D.R.1    Bruss, V.2    Ganem, D.3
  • 70
    • 0028037170 scopus 로고
    • The large surface protein of duck hepatitis B virus is phosphorylated in the pre-S domain
    • Grgacic EV, Anderson DA. The large surface protein of duck hepatitis B virus is phosphorylated in the pre-S domain. J Virol 1994; 68: 7344-7350
    • (1994) J Virol , vol.68 , pp. 7344-7350
    • Grgacic, E.V.1    Anderson, D.A.2
  • 71
    • 0031744107 scopus 로고    scopus 로고
    • Host cell-virus cross talk: Phosphorylation of a hepatitis B virus envelope protein mediates intracellular signaling
    • Rothmann K, Schnolzer M, Radziwill G, Hildt E, Moelling K, Schaller H. Host cell-virus cross talk: phosphorylation of a hepatitis B virus envelope protein mediates intracellular signaling. J Virol 1998; 72:10138-10147
    • (1998) J Virol , vol.72 , pp. 10138-10147
    • Rothmann, K.1    Schnolzer, M.2    Radziwill, G.3    Hildt, E.4    Moelling, K.5    Schaller, H.6
  • 72
    • 0034021679 scopus 로고    scopus 로고
    • Novel cell permeable motif derived from the PreS2-domain of hepatitis-B virus surface antigens
    • Oess S, Hildt E. Novel cell permeable motif derived from the PreS2-domain of hepatitis-B virus surface antigens. Gene Ther 2000; 7: 750-758
    • (2000) Gene Ther , vol.7 , pp. 750-758
    • Oess, S.1    Hildt, E.2
  • 73
    • 0028236042 scopus 로고
    • Post-translational alterations in transmembrane topology of the hepatitis B virus large envelope protein
    • Bruss V, Lu. X, Thomssen R, Gerlich WH. Post-translational alterations in transmembrane topology of the hepatitis B virus large envelope protein. EMBO J 1994; 13: 2273-2279
    • (1994) EMBO J , vol.13 , pp. 2273-2279
    • Bruss, V.1    Lu, X.2    Thomssen, R.3    Gerlich, W.H.4
  • 74
    • 0035933758 scopus 로고    scopus 로고
    • Dual topology of the hepatitis B virus large envelope protein: Determinants influencing post-translational pre-S translocation
    • Lambert C, Prange R. Dual topology of the hepatitis B virus large envelope protein: determinants influencing post-translational pre-S translocation. J Biol Chem 2001; 276: 22265-22272
    • (2001) J Biol Chem , vol.276 , pp. 22265-22272
    • Lambert, C.1    Prange, R.2
  • 75
    • 0032520549 scopus 로고    scopus 로고
    • Intracellular retention of duck hepatitis B virus large surface protein is independent of preS topology
    • Gazina EV, Lin B, Gallina A, Milanesi G, Anderson DA. Intracellular retention of duck hepatitis B virus large surface protein is independent of preS topology. Virology 1998; 242: 266-278
    • (1998) Virology , vol.242 , pp. 266-278
    • Gazina, E.V.1    Lin, B.2    Gallina, A.3    Milanesi, G.4    Anderson, D.A.5
  • 76
    • 0025980689 scopus 로고
    • Morphogenetic and regulatory effects of mutations in the envelope proteins of an avian hepadnavirus
    • Summers J, Smith PM, Huang MJ, Yu MS. Morphogenetic and regulatory effects of mutations in the envelope proteins of an avian hepadnavirus. J Virol 1991; 65: 1310-1317
    • (1991) J Virol , vol.65 , pp. 1310-1317
    • Summers, J.1    Smith, P.M.2    Huang, M.J.3    Yu, M.S.4
  • 77
    • 3242704987 scopus 로고    scopus 로고
    • Superinfection exclusion in duck hepatitis B virus infection is mediated by the large surface antigen
    • Walters KA, Joyce MA, Addison WR, Fischer KP, Tyrrell DL. Superinfection exclusion in duck hepatitis B virus infection is mediated by the large surface antigen. J Virol 2004; 78: 7925-7937
    • (2004) J Virol , vol.78 , pp. 7925-7937
    • Walters, K.A.1    Joyce, M.A.2    Addison, W.R.3    Fischer, K.P.4    Tyrrell, D.L.5
  • 78
    • 0035861455 scopus 로고    scopus 로고
    • Calcium signaling by HBx protein in hepatitis B virus DNA replication
    • Bouchard MJ, Wang LH, Schneider RJ. Calcium signaling by HBx protein in hepatitis B virus DNA replication. Science 2001; 294: 2376-2378
    • (2001) Science , vol.294 , pp. 2376-2378
    • Bouchard, M.J.1    Wang, L.H.2    Schneider, R.J.3
  • 79
    • 0346155880 scopus 로고    scopus 로고
    • A duck hepatitis B virus strain with a knockout mutation in the putative X ORF shows similar infectivity and in vivo growth characteristics to wild-type virus
    • Meier P, Scougall CA, Will H, Burrell CJ, Jilbert AR. A duck hepatitis B virus strain with a knockout mutation in the putative X ORF shows similar infectivity and in vivo growth characteristics to wild-type virus. Virology 2003; 317: 291-298
    • (2003) Virology , vol.317 , pp. 291-298
    • Meier, P.1    Scougall, C.A.2    Will, H.3    Burrell, C.J.4    Jilbert, A.R.5
  • 80
    • 0024385188 scopus 로고
    • Infection and uptake of duck hepatitis B virus by duck hepatocytes maintained in the presence of dimethyl sulfoxide
    • Pugh JC, Summers JW. Infection and uptake of duck hepatitis B virus by duck hepatocytes maintained in the presence of dimethyl sulfoxide. Virology 1989; 172: 564-572
    • (1989) Virology , vol.172 , pp. 564-572
    • Pugh, J.C.1    Summers, J.W.2
  • 81
    • 0029070471 scopus 로고
    • Susceptibility to duck hepatitis B virus infection is associated with the presence of cell surface receptor sites that efficiently bind viral particles
    • Pugh JC, Di Q, Mason WS, Simmons H. Susceptibility to duck hepatitis B virus infection is associated with the presence of cell surface receptor sites that efficiently bind viral particles. J Virol 1995; 69: 4814-4822
    • (1995) J Virol , vol.69 , pp. 4814-4822
    • Pugh, J.C.1    Di, Q.2    Mason, W.S.3    Simmons, H.4
  • 82
    • 0023791032 scopus 로고
    • Replication of duck hepatitis B virus in two differentiated human hepatoma cell lines after transfection with cloned viral DNA
    • Hirsch R, Colgrove R, Ganem D. Replication of duck hepatitis B virus in two differentiated human hepatoma cell lines after transfection with cloned viral DNA. Virology 1988; 167: 136-142
    • (1988) Virology , vol.167 , pp. 136-142
    • Hirsch, R.1    Colgrove, R.2    Ganem, D.3
  • 83
    • 0028295258 scopus 로고
    • A cell surface protein that binds avian hepatitis B virus particles
    • Kuroki K, Cheung R, Marion PL, Ganem D. A cell surface protein that binds avian hepatitis B virus particles. J Virol 1994; 68: 2091-2096
    • (1994) J Virol , vol.68 , pp. 2091-2096
    • Kuroki, K.1    Cheung, R.2    Marion, P.L.3    Ganem, D.4
  • 84
    • 0031682561 scopus 로고    scopus 로고
    • Carboxypeptidase D (gp180), a Golgi-resident protein, functions in the attachment and entry of avian hepatitis B viruses
    • Breiner KM, Urban S, Schaller H. Carboxypeptidase D (gp180), a Golgi-resident protein, functions in the attachment and entry of avian hepatitis B viruses. J Virol 1998; 72: 8098-8104
    • (1998) J Virol , vol.72 , pp. 8098-8104
    • Breiner, K.M.1    Urban, S.2    Schaller, H.3
  • 85
    • 0034654306 scopus 로고    scopus 로고
    • Receptor recognition by a hepatitis B virus reveals a novel mode of high affinity virus-receptor interaction
    • Urban S, Schwarz C, Marx UC, Zentgraf H, Schaller H, Multhaup G. Receptor recognition by a hepatitis B virus reveals a novel mode of high affinity virus-receptor interaction. EMBO J 2000; 19: 1217-1227
    • (2000) EMBO J , vol.19 , pp. 1217-1227
    • Urban, S.1    Schwarz, C.2    Marx, U.C.3    Zentgraf, H.4    Schaller, H.5    Multhaup, G.6
  • 86
    • 0036146250 scopus 로고    scopus 로고
    • Inhibition of duck hepatitis B virus infection by a myristoylated pre-S peptide of the large viral surface protein
    • Urban S, Gripon P. Inhibition of duck hepatitis B virus infection by a myristoylated pre-S peptide of the large viral surface protein. J Virol 2002; 76: 1986-1990
    • (2002) J Virol , vol.76 , pp. 1986-1990
    • Urban, S.1    Gripon, P.2
  • 87
    • 0031666031 scopus 로고    scopus 로고
    • Avian hepatitis B virus infection is initiated by the interaction of a distinct pre-S subdomain with the cellular receptor gp180
    • Urban S, Breiner KM, Fehler F, Klingmuller U, Schaller H. Avian hepatitis B virus infection is initiated by the interaction of a distinct pre-S subdomain with the cellular receptor gp180. J Virol 1998; 72: 8089-8097
    • (1998) J Virol , vol.72 , pp. 8089-8097
    • Urban, S.1    Breiner, K.M.2    Fehler, F.3    Klingmuller, U.4    Schaller, H.5
  • 89
    • 0026506254 scopus 로고
    • Duck hepatitis B virus infection of hepatocytes is not dependent on low pH
    • Rigg RJ, Schaller H. Duck hepatitis B virus infection of hepatocytes is not dependent on low pH. J Virol 1992; 66: 2829-2836
    • (1992) J Virol , vol.66 , pp. 2829-2836
    • Rigg, R.J.1    Schaller, H.2
  • 90
    • 27744573975 scopus 로고    scopus 로고
    • A hydrophobic domain in the large envelope protein is essential for fusion of duck hepatitis B virus at the late endosome
    • Chojnacki J, Anderson DA, Grgacic EV. A hydrophobic domain in the large envelope protein is essential for fusion of duck hepatitis B virus at the late endosome. J Virol 2005; 79: 14945-14955
    • (2005) J Virol , vol.79 , pp. 14945-14955
    • Chojnacki, J.1    Anderson, D.A.2    Grgacic, E.V.3
  • 91
    • 0027272784 scopus 로고
    • Analysis of the earliest steps of hepadnavirus replication: Genome repair after infectious entry into hepatocytes does not depend on viral polymerase activity
    • Kock J, Schlicht HJ. Analysis 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
    • (1993) J Virol , vol.67 , pp. 4867-4874
    • Kock, J.1    Schlicht, H.J.2
  • 94
    • 0030589467 scopus 로고    scopus 로고
    • Kinetics of duck hepatitis B virus infection following low dose virus inoculation: One virus DNA genome is infectious in neonatal ducks
    • Jilbert AR, Miller DS, Scougall CA, Turnbull H, Burrell CJ. Kinetics of duck hepatitis B virus infection following low dose virus inoculation: one virus DNA genome is infectious in neonatal ducks. Virology 1996; 226: 338-345
    • (1996) Virology , vol.226 , pp. 338-345
    • Jilbert, A.R.1    Miller, D.S.2    Scougall, C.A.3    Turnbull, H.4    Burrell, C.J.5
  • 95
    • 0347634427 scopus 로고    scopus 로고
    • Rapid production of neutralizing antibody leads to transient hepadnavirus infection
    • Zhang YY, Summers J. Rapid production of neutralizing antibody leads to transient hepadnavirus infection. J Virol 2004; 78: 1195-1201
    • (2004) J Virol , vol.78 , pp. 1195-1201
    • Zhang, Y.Y.1    Summers, J.2
  • 96
    • 0023226446 scopus 로고
    • Duck hepatitis B virus replicates in the yolk sac of developing embryos
    • Tagawa M, Robinson WS, Marion PL. Duck hepatitis B virus replicates in the yolk sac of developing embryos. J Virol 1987; 61: 2273-2279
    • (1987) J Virol , vol.61 , pp. 2273-2279
    • Tagawa, M.1    Robinson, W.S.2    Marion, P.L.3
  • 97
    • 0032506099 scopus 로고    scopus 로고
    • Competition in vivo between a cytopathic variant and a wild-type duck hepatitis B virus
    • Lenhoff RJ, Luscombe CA, Summers J. Competition in vivo between a cytopathic variant and a wild-type duck hepatitis B virus. Virology 1998; 251: 85-95
    • (1998) Virology , vol.251 , pp. 85-95
    • Lenhoff, R.J.1    Luscombe, C.A.2    Summers, J.3
  • 98
    • 0343569832 scopus 로고    scopus 로고
    • Endotoxin stimulates liver macrophages to release mediators that inhibit an early step in hepadnavirus replication
    • Klocker U, Schultz U, Schaller H, Protzer U. Endotoxin stimulates liver macrophages to release mediators that inhibit an early step in hepadnavirus replication. J Virol 2000; 74: 5525-5533
    • (2000) J Virol , vol.74 , pp. 5525-5533
    • Klocker, U.1    Schultz, U.2    Schaller, H.3    Protzer, U.4
  • 100
    • 17444431576 scopus 로고    scopus 로고
    • Effect of antiviral treatment with entecavir on age- and dose-related outcomes of duck hepatitis B virus infection
    • Foster WK, Miller DS, Scougall CA, Kotlarski I, Colonno RJ, Jilbert AR. Effect of antiviral treatment with entecavir on age- and dose-related outcomes of duck hepatitis B virus infection. J Virol 2005; 79: 5819-5832
    • (2005) J Virol , vol.79 , pp. 5819-5832
    • Foster, W.K.1    Miller, D.S.2    Scougall, C.A.3    Kotlarski, I.4    Colonno, R.J.5    Jilbert, A.R.6
  • 101
    • 0031964789 scopus 로고    scopus 로고
    • Protective efficacy of DNA vaccines against duck hepatitis B virus infection
    • Triyatni M, Jilbert AR, Qiao M, Miller DS, Burrell CJ. Protective efficacy of DNA vaccines against duck hepatitis B virus infection. J Virol 1998; 72: 84-94
    • (1998) J Virol , vol.72 , pp. 84-94
    • Triyatni, M.1    Jilbert, A.R.2    Qiao, M.3    Miller, D.S.4    Burrell, C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.