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Volumn 71, Issue 12, 1997, Pages 9434-9441

Dual topology of the large envelope protein of duck hepatitis B virus: Determinants preventing pre-S translocation and glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN;

EID: 0030731674     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.12.9434-9441.1997     Document Type: Article
Times cited : (43)

References (29)
  • 1
    • 0028013056 scopus 로고
    • Mapping a region of the large envelope protein required for hepatitis B virion maturation
    • Bruss, V., and R. Thomssen. 1994. Mapping a region of the large envelope protein required for hepatitis B virion maturation. J. Virol. 68:1643-1650.
    • (1994) J. Virol. , vol.68 , pp. 1643-1650
    • Bruss, V.1    Thomssen, R.2
  • 2
    • 0028236042 scopus 로고
    • Posttranslational alterations in transmembrane topology of the hepatitis B virus large envelope protein
    • Brass, V., X. Lu, R. Thomssen, and W. 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
    • Brass, V.1    Lu, X.2    Thomssen, R.3    Gerlich, W.4
  • 3
    • 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
  • 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
    • 0028037170 scopus 로고
    • The large surface protein of duck hepatitis B virus is phosphorylated in the pre-S domain
    • Grgacic, E. V. L., and D. A. Anderson. 1994. The large surface protein of duck hepatitis B virus is phosphorylated in the pre-S domain. J. Virol. 68:7344-7350.
    • (1994) J. Virol. , vol.68 , pp. 7344-7350
    • Grgacic, E.V.L.1    Anderson, D.A.2
  • 6
    • 0031015208 scopus 로고    scopus 로고
    • Topology of the large envelope protein of duck hepatitis B virus suggests a mechanism for membrane translocation during particle morphogenesis
    • Guo, J. T., and J. C. Pugh. 1997. Topology of the large envelope protein of duck hepatitis B virus suggests a mechanism for membrane translocation during particle morphogenesis. J. Virol. 71:1107-1114.
    • (1997) J. Virol. , vol.71 , pp. 1107-1114
    • Guo, J.T.1    Pugh, J.C.2
  • 7
  • 8
    • 0000523194 scopus 로고
    • Surface proteins of hepatitis B viruses
    • A. McLachlan (ed.), CRC Press, Boca Raton, Fla.
    • Heermann, K. H., and W. H. Gerlich. 1991. Surface proteins of hepatitis B viruses, p. 145-169. In A. McLachlan (ed.), Molecular biology of the hepatitis B virus. CRC Press, Boca Raton, Fla.
    • (1991) Molecular Biology of the Hepatitis B Virus , pp. 145-169
    • Heermann, K.H.1    Gerlich, W.H.2
  • 10
    • 0023663186 scopus 로고
    • Expression and replication of the hepatitis B virus genome under foreign promoter control
    • Junker, M., P. Galle, and H. Schaller. 1987. Expression and replication of the hepatitis B virus genome under foreign promoter control. Nucleic Acids Res. 15:10117-10132.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 10117-10132
    • Junker, M.1    Galle, P.2    Schaller, H.3
  • 12
    • 0027430748 scopus 로고
    • Hepadnavirus infection requires interaction between the viral pre-S domain and a specific hepatocellular receptor
    • Klingmüller, U., and H. Schaller. 1993. Hepadnavirus infection requires interaction between the viral pre-S domain and a specific hepatocellular receptor. J. Virol. 67:7414-7422.
    • (1993) J. Virol. , vol.67 , pp. 7414-7422
    • Klingmüller, U.1    Schaller, H.2
  • 13
    • 1842280007 scopus 로고    scopus 로고
    • Unpublished data
    • 12a. Kuhn, C. Unpublished data.
    • Kuhn, C.1
  • 14
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., J. G. Donaldson, A. Schweizer, E. G. Berger, H. P. Hauri, L. C. Yuan, and R. D. Klausner. 1990. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60:821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 15
    • 0030391205 scopus 로고    scopus 로고
    • Hepatitis B virus morphogenesis
    • Nassal, M. 1996. Hepatitis B virus morphogenesis. Curr. Top. Microbiol. Immunol. 214:297-337.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 297-337
    • Nassal, M.1
  • 16
    • 0022538381 scopus 로고
    • Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus
    • Neurath, A. R., B. H. 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, B.H.2    Strick, N.3    Parker, K.4
  • 17
    • 0025015646 scopus 로고
    • Fine-tuning the topology of a polytopic membrane protein: Role of positively and negatively charged amino acids
    • Nilsson, I., and G. von Heijne. 1990. Fine-tuning the topology of a polytopic membrane protein: role of positively and negatively charged amino acids. Cell 62:1135-1141.
    • (1990) Cell , vol.62 , pp. 1135-1141
    • Nilsson, I.1    Von Heijne, G.2
  • 19
    • 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
  • 20
    • 0023353201 scopus 로고
    • The structure of hepatitis B surface antigen and its antigenic sites
    • Peterson, D. L. 1987. The structure of hepatitis B surface antigen and its antigenic sites. BioAssays 6:258-262.
    • (1987) BioAssays , vol.6 , pp. 258-262
    • Peterson, D.L.1
  • 21
    • 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
  • 22
    • 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
  • 23
    • 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
  • 27
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne, G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 28
    • 0028300388 scopus 로고
    • Hepadnaviral P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription
    • Weber, M., V. Bronsema, H. Bartos, A. Bosserhoff, R. Bartenschlager, and H. Schaller. 1994. Hepadnaviral P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription. J. Virol. 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
  • 29
    • 0026090336 scopus 로고
    • Peptide mapping of neutralizing and nonneutralizing epitopes of duck hepatitis B virus pre-S polypeptide
    • Yuasa, S., Cheung, R. C., 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.