메뉴 건너뛰기




Volumn 71, Issue 2, 1997, Pages 1107-1114

Topology of the large envelope protein of duck hepatitis B virus suggests a mechanism for membrane translocation during particle morphogenesis

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS ENVELOPE PROTEIN;

EID: 0031015208     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.2.1107-1114.1997     Document Type: Article
Times cited : (36)

References (36)
  • 1
    • 0028013056 scopus 로고
    • Mapping a region of the large envelope protein required for hepatitis B virus maturation
    • Bruss, V., and R. Thomssen. 1994. Mapping a region of the large envelope protein required for hepatitis B virus maturation. J. Virol. 68:1643-1650.
    • (1994) J. Virol. , vol.68 , pp. 1643-1650
    • Bruss, V.1    Thomssen, R.2
  • 2
    • 0028874697 scopus 로고
    • Functions of the internal pre-S domain of the large surface protein in hepatitis B virus particle morphogenesis
    • Bruss, V., and K. Vieluf. 1995. Functions of the internal pre-S domain of the large surface protein in hepatitis B virus particle morphogenesis. J. Virol. 69:6652-6657.
    • (1995) J. Virol. , vol.69 , pp. 6652-6657
    • Bruss, V.1    Vieluf, K.2
  • 3
    • 0028236042 scopus 로고
    • Posttranslational alterations in transmembrane topology of the hepatitis B virus large envelope protein
    • Bruss, V., L. Xuanyong, R. Thomssen, and W. H. Gerlich. 1994. Posttranslational alterations in transmembrane topology of the hepatitis B virus large envelope protein. EMBO J. 13:2273-2279.
    • (1994) EMBO J. , vol.13 , pp. 2273-2279
    • Bruss, V.1    Xuanyong, L.2    Thomssen, R.3    Gerlich, W.H.4
  • 4
    • 0025314572 scopus 로고
    • Efficient duck hepatitis B virus production by an avian liver tumor cell line
    • Condreay, L. D., C. E. Aldrich, L. Coates, W. S. Mason, and T. T. Wu. 1990. Efficient duck hepatitis B virus production by an avian liver tumor cell line. J. Virol. 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
  • 5
    • 0026655316 scopus 로고
    • Bacterial protein translocation: Kinetic and thermodynamic role of ATP and the protonmotive force
    • Driessen, A. J. M. 1992. Bacterial protein translocation: kinetic and thermodynamic role of ATP and the protonmotive force. Trends Biochem. Sci. 17:219-223.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 219-223
    • Driessen, A.J.M.1
  • 6
    • 0022573411 scopus 로고
    • Hepatitis B surface antigen: An unusual secreted protein initially synthesized as a transmembrane polypeptide
    • Eble, B. E., V. R. Lingappa, and D. Ganem. 1986. Hepatitis B surface antigen: an unusual secreted protein initially synthesized as a transmembrane polypeptide. Mol. Cell. Biol. 6:1454-1463.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1454-1463
    • Eble, B.E.1    Lingappa, V.R.2    Ganem, D.3
  • 7
    • 0020265940 scopus 로고
    • Structure of the hepatitis B surface antigen. Characterization of the lipid components and their association with viral proteins
    • Gavilanes, F., A. Gonzales-Ros, and D. Peterson. 1982. Structure of the hepatitis B surface antigen. Characterization of the lipid components and their association with viral proteins. J. Biol. Chem. 257:7770-7777.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7770-7777
    • Gavilanes, F.1    Gonzales-Ros, A.2    Peterson, D.3
  • 8
    • 0028871747 scopus 로고
    • Receptor-induced conformational changes in the subgroup a avian leukosis and sarcoma virus envelope glycoprotein
    • Gilbert, J., L. Hernandez, J. Balliet, P. Bates, and J. White. 1995. Receptor-induced conformational changes in the subgroup A avian leukosis and sarcoma virus envelope glycoprotein. J. Virol. 69:7410-7415.
    • (1995) J. Virol. , vol.69 , pp. 7410-7415
    • Gilbert, J.1    Hernandez, L.2    Balliet, J.3    Bates, P.4    White, J.5
  • 9
    • 0027367627 scopus 로고
    • Protein translocation across the endoplasmic reticulum: A tunnel with toll booths at entry and exit
    • Gilmore, R. 1993. Protein translocation across the endoplasmic reticulum: a tunnel with toll booths at entry and exit. Cell 75:589-592.
    • (1993) Cell , vol.75 , pp. 589-592
    • Gilmore, R.1
  • 10
    • 0002843412 scopus 로고
    • Model for the protein arrangement in HBsAg particles based on physical and chemical studies
    • A. J. Zuckerman (ed.), Alan R. Liss, Inc., New York, N.Y
    • Guerrero, E., F. Gavilanes, and D. L. Peterson. 1988. Model for the protein arrangement in HBsAg particles based on physical and chemical studies, p. 606-613. In A. J. Zuckerman (ed.), Viral hepatitis and liver disease. Alan R. Liss, Inc., New York, N.Y.
    • (1988) Viral Hepatitis and Liver Disease , pp. 606-613
    • Guerrero, E.1    Gavilanes, F.2    Peterson, D.L.3
  • 11
    • 0000523194 scopus 로고
    • Surface proteins of hepatitis B viruses
    • A. McLachlan (ed.), CRC Press, Inc., Boca Raton, Fla.
    • Heermann, K.-H., and W. H. Gerlich. 1991. Surface proteins of hepatitis B viruses, p. 109-143. In A. McLachlan (ed.), Molecular biology of the hepatitis B virus. CRC Press, Inc., Boca Raton, Fla.
    • (1991) Molecular Biology of the Hepatitis B Virus , pp. 109-143
    • Heermann, K.-H.1    Gerlich, W.H.2
  • 12
    • 0026664025 scopus 로고
    • Unpacking the incoming influenza virus
    • Helenius, A. 1992. Unpacking the incoming influenza virus. Cell 69:577-578.
    • (1992) Cell , vol.69 , pp. 577-578
    • Helenius, A.1
  • 13
    • 0027430748 scopus 로고
    • Hepadnavirus infection requires interaction between the virus pre-S domain and a specific hepatocellular receptor
    • Klingmuller, U., and H. Schaller. 1993. Hepadnavirus infection requires interaction between the virus pre-S domain and a specific hepatocellular receptor. J. Virol. 67:7414-7422.
    • (1993) J. Virol. , vol.67 , pp. 7414-7422
    • Klingmuller, U.1    Schaller, H.2
  • 14
    • 0025277448 scopus 로고
    • Efficient translocation of positively charged residues of M13 precoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion
    • Kuhn, A., H.-Y. Zhu, and R. E. Dalbey. 1990. Efficient translocation of positively charged residues of M13 precoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion. EMBO J. 9:2385-2389.
    • (1990) EMBO J. , vol.9 , pp. 2385-2389
    • Kuhn, A.1    Zhu, H.-Y.2    Dalbey, R.E.3
  • 15
    • 0003156040 scopus 로고
    • The influenza a virus M2 ion channel protein and its role in the influenza virus life cycle
    • E. Wimmer (ed.), Cold Spring Harbor Press, Cold Spring Harbor, N.Y
    • Lamb, R., L. Holsinger, and L. Pinto. 1994. The influenza A virus M2 ion channel protein and its role in the influenza virus life cycle, p. 303-321. In E. Wimmer (ed.), Cellular receptors for animal viruses. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
    • (1994) Cellular Receptors for Animal Viruses , pp. 303-321
    • Lamb, R.1    Holsinger, L.2    Pinto, L.3
  • 16
    • 0028334395 scopus 로고
    • Coordinate regulation of replication and virus assembly by the large envelope protein of an avian hepadnavirus
    • Lenhoff, R., and J. Summers. 1994. Coordinate regulation of replication and virus assembly by the large envelope protein of an avian hepadnavirus. J. Virol. 68:4565-4571.
    • (1994) J. Virol. , vol.68 , pp. 4565-4571
    • Lenhoff, R.1    Summers, J.2
  • 17
    • 0021342069 scopus 로고
    • Nucleotide sequence of a cloned duck hepatitis B virus genome: Comparison with woodchuck and human hepatitis B virus sequences
    • Mandart, E., A. Kay, and F. Galibert. 1984. Nucleotide sequence of a cloned duck hepatitis B virus genome: comparison with woodchuck and human hepatitis B virus sequences. J. Virol. 49:782-792.
    • (1984) J. Virol. , vol.49 , pp. 782-792
    • Mandart, E.1    Kay, A.2    Galibert, F.3
  • 18
    • 0029670548 scopus 로고    scopus 로고
    • Snapshots of membrane-translocating proteins
    • Martoglio, B, and B. Dobberstein. 1996. Snapshots of membrane-translocating proteins. Trends Cell Biol. 6:142-147.
    • (1996) Trends Cell Biol. , vol.6 , pp. 142-147
    • Martoglio, B.1    Dobberstein, B.2
  • 19
    • 0022538381 scopus 로고
    • Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus
    • Neurath, A. R., S. B. Kent, N. Strick, and K. Parker. 1986. Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell 46:429-436.
    • (1986) Cell , vol.46 , pp. 429-436
    • Neurath, A.R.1    Kent, S.B.2    Strick, N.3    Parker, K.4
  • 20
    • 0025785179 scopus 로고
    • Inhibition of duck hepatitis B virus infection by lysosomotropic agents
    • Offensperger, W. B., S. Offensperger, E. Walter, H. E. Blum, and W. Gerok. 1991. Inhibition of duck hepatitis B virus infection by lysosomotropic agents. Virology 183:415-418.
    • (1991) Virology , vol.183 , pp. 415-418
    • Offensperger, W.B.1    Offensperger, S.2    Walter, E.3    Blum, H.E.4    Gerok, W.5
  • 21
    • 0028265897 scopus 로고
    • A dramatic shift in the transmembrane topology of a viral envelope glycoprotein accompanies hepatitis B viral morphogenesis
    • Ostapchuk, P., P. Hearing, and D. Ganem. 1994. A dramatic shift in the transmembrane topology of a viral envelope glycoprotein accompanies hepatitis B viral morphogenesis. EMBO J. 13:1048-1057.
    • (1994) EMBO J. , vol.13 , pp. 1048-1057
    • Ostapchuk, P.1    Hearing, P.2    Ganem, D.3
  • 22
    • 0023177636 scopus 로고
    • The pre-S1 protein of hepatitis B virus is acylated at its amino terminus with myristic acid
    • Persing, D. H., H. E. Varmus, and D. Ganem. 1987. The pre-S1 protein of hepatitis B virus is acylated at its amino terminus with myristic acid. J. Virol. 61:1672-1677.
    • (1987) J. Virol. , vol.61 , pp. 1672-1677
    • Persing, D.H.1    Varmus, H.E.2    Ganem, D.3
  • 23
    • 0024603006 scopus 로고
    • Human liver plasma membranes contain receptors for the hepatitis B virus pre-S1 region and, via polymerized human serum albumin, for the pre-S2 region J
    • Pontisso, P., M. A. Petit, M. J. Bankowski, and M. E. Peeples. 1989. Human liver plasma membranes contain receptors for the hepatitis B virus pre-S1 region and, via polymerized human serum albumin, for the pre-S2 region J. Virol. 63:1981-1988.
    • (1989) Virol. , vol.63 , pp. 1981-1988
    • Pontisso, P.1    Petit, M.A.2    Bankowski, M.J.3    Peeples, M.E.4
  • 24
    • 0028859149 scopus 로고
    • Novel transmembrane topology of the hepatitis B virus envelope proteins
    • Prange, R., and R. E. Streeck. 1995. Novel transmembrane topology of the hepatitis B virus envelope proteins. EMBO J. 14:247-256.
    • (1995) EMBO J. , vol.14 , pp. 247-256
    • Prange, R.1    Streeck, R.E.2
  • 25
    • 1842324189 scopus 로고    scopus 로고
    • Unpublished data
    • 24a.Pugh, J. C. Unpublished data.
    • Pugh, J.C.1
  • 26
    • 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, J. C., Q. Di, W. S. Mason, and H. Simmons. 1995. Susceptibility to duck hepatitis B virus infection is associated with the presence of cell surface receptor sites that efficiently bind viral particles. J. Virol. 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
  • 27
    • 0023233802 scopus 로고
    • Characterization of a pre-S polypeptide on the surfaces of infectious avian hepadnavirus particles
    • Pugh, J. C., J. J. Sninsky, J. W. Summers, and E. Schaeffer. 1987. Characterization of a pre-S polypeptide on the surfaces of infectious avian hepadnavirus particles. J. Virol. 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
  • 28
    • 0026506254 scopus 로고
    • Duck hepatitis B virus infection of hepatocytes is not dependent on low pH
    • Rigg, R. J., and H. Schaller. 1992. Duck hepatitis B virus infection of hepatocytes is not dependent on low pH. J. Virol. 66:2829-2836.
    • (1992) J. Virol. , vol.66 , pp. 2829-2836
    • Rigg, R.J.1    Schaller, H.2
  • 29
    • 1842347254 scopus 로고    scopus 로고
    • Personal communication
    • 27a.Schaller, H. Personal communication.
    • Schaller, H.1
  • 30
    • 0023194213 scopus 로고
    • Biochemical and immunological characterization of the duck hepatitis B virus envelope proteins
    • Schlicht, H. J., C. Kuhn, B. Guhr, R. J. Mattaliano, and H. Schaller. 1987. Biochemical and immunological characterization of the duck hepatitis B virus envelope proteins. J. Virol. 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
  • 31
    • 0024245271 scopus 로고
    • Secreted HBsAg polypeptides are derived from a transmembrane precursor
    • Simon, K., V. Lingappa, and D. Ganem. 1988. Secreted HBsAg polypeptides are derived from a transmembrane precursor. J. Cell Biol. 107:2163-2168.
    • (1988) J. Cell Biol. , vol.107 , pp. 2163-2168
    • Simon, K.1    Lingappa, V.2    Ganem, D.3
  • 32
    • 0026773810 scopus 로고
    • A topological model for hepatitis B surface antigen
    • Stirk, H., J. Thornton, and C. Howard. 1992. A topological model for hepatitis B surface antigen. Intervirology 33:148-158.
    • (1992) Intervirology , vol.33 , pp. 148-158
    • Stirk, H.1    Thornton, J.2    Howard, C.3
  • 33
    • 0025980689 scopus 로고
    • Morphogenetic and regulatory effects of mutations in the envelope proteins of an avian hepadnavirus
    • Summers, J., P. M. Smith, M. J. Huang, and M. S. Yu. 1991. Morphogenetic and regulatory effects of mutations in the envelope proteins of an avian hepadnavirus. J. Virol. 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
  • 34
    • 0022504551 scopus 로고
    • In vitro experimental infection of primary duck hepatocyte cultures with duck hepatitis B virus
    • Tuttleman. J. S., J. C. Pugh, and J. W. Summers. 1986. In vitro experimental infection of primary duck hepatocyte cultures with duck hepatitis B virus. J. Virol. 58:17-25.
    • (1986) J. Virol. , vol.58 , pp. 17-25
    • Tuttleman, J.S.1    Pugh, J.C.2    Summers, J.W.3
  • 35
    • 0002641729 scopus 로고
    • Fusion of influenza virus in endosomes: Role of the hemagglutinin
    • E. Wimmer (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
    • White, J. 1994. Fusion of influenza virus in endosomes: role of the hemagglutinin, p. 281-301. In E. Wimmer (ed.), Cellular receptors for animal viruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) Cellular Receptors for Animal Viruses , pp. 281-301
    • White, J.1
  • 36
    • 0026090336 scopus 로고
    • Peptide mapping of neutralizing and nonneutralizing epitopes of duck hepatitis B virus pre-S polypeptide
    • Yuasa, S., R. C. Cheung, Q. Pham, W. S. Robinson, and P. L. Marion. 1991. Peptide mapping of neutralizing and nonneutralizing epitopes of duck hepatitis B virus pre-S polypeptide. Virology 181:14-21.
    • (1991) Virology , vol.181 , pp. 14-21
    • Yuasa, S.1    Cheung, R.C.2    Pham, Q.3    Robinson, W.S.4    Marion, P.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.