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Volumn 261, Issue 1, 1999, Pages 133-142

Fusogenic activity of hepadnavirus peptides corresponding to sequences downstream of the putative cleavage site

Author keywords

[No Author keywords available]

Indexed keywords

1,6 DIPHENYL 1,3,5 HEXATRIENE; LIPOSOME; SYNTHETIC PEPTIDE; VIRUS FUSION PROTEIN;

EID: 0343984655     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1999.9823     Document Type: Article
Times cited : (24)

References (44)
  • 1
    • 0000788308 scopus 로고
    • Kinetics of divalent cation induced fusion of phosphatidylserine vesicles: Correlation between fusogenic properties and binding affinities
    • Bentz J., Düzgünes N., Nir S. Kinetics of divalent cation induced fusion of phosphatidylserine vesicles: Correlation between fusogenic properties and binding affinities. Biochemistry. 22:1983;3320-3330.
    • (1983) Biochemistry , vol.22 , pp. 3320-3330
    • Bentz, J.1    Düzgünes, N.2    Nir, S.3
  • 2
    • 0021099319 scopus 로고
    • Clathrin-induced pH-dependent fusion of phosphatidylcholine vesicles
    • Blumenthal R., Henkart M., Steer C. J. Clathrin-induced pH-dependent fusion of phosphatidylcholine vesicles. J. Biol. Chem. 258:1983;3409-3415.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3409-3415
    • Blumenthal, R.1    Henkart, M.2    Steer, C.J.3
  • 4
    • 0031682561 scopus 로고    scopus 로고
    • Carboxypeptidase D (gp180), a Golgi-resident protein, functions in the attachment and entry of avian hepatitis B viruses
    • Breiner K. M., Urban S., Schaller H. Carboxypeptidase D (gp180), a Golgi-resident protein, functions in the attachment and entry of avian hepatitis B viruses. J. Virol. 72:1998;8098-8104.
    • (1998) J. Virol. , vol.72 , pp. 8098-8104
    • Breiner, K.M.1    Urban, S.2    Schaller, H.3
  • 5
    • 0032478582 scopus 로고    scopus 로고
    • Structural plasticity of the feline leukaemia virus fusion peptide: A circular dichroism study
    • Davies S. M. A., Kelly S. M., Price N. C., Bradshaw J. P. Structural plasticity of the feline leukaemia virus fusion peptide: A circular dichroism study. FEBS Lett. 425:1998;415-418.
    • (1998) FEBS Lett. , vol.425 , pp. 415-418
    • Davies, S.M.A.1    Kelly, S.M.2    Price, N.C.3    Bradshaw, J.P.4
  • 6
    • 0030682144 scopus 로고    scopus 로고
    • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion
    • Durell S. R., Martin I., Ruysschaert J.-M., Shai Y., Blumenthal R. What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion. Mol. Membr. Biol. 14:1997;97-112.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 97-112
    • Durell, S.R.1    Martin, I.2    Ruysschaert, J.-M.3    Shai, Y.4    Blumenthal, R.5
  • 7
    • 0023657261 scopus 로고
    • Lipid mixing during membrane aggregation and fusion. Why fusion assays disagree
    • Düzgünes N., Allen T. M., Fedor J., Papahadjopoulos D. Lipid mixing during membrane aggregation and fusion. Why fusion assays disagree. Biochemistry. 26:1987;8435-8442.
    • (1987) Biochemistry , vol.26 , pp. 8435-8442
    • Düzgünes, N.1    Allen, T.M.2    Fedor, J.3    Papahadjopoulos, D.4
  • 8
    • 0026645243 scopus 로고
    • Membrane destabilization by N-terminal peptides of viral envelope proteins
    • Düzgünes N., Shavnin S. A. Membrane destabilization by N-terminal peptides of viral envelope proteins. J. Membr. Biol. 128:1992;71-80.
    • (1992) J. Membr. Biol. , vol.128 , pp. 71-80
    • Düzgünes, N.1    Shavnin, S.A.2
  • 9
    • 0021890825 scopus 로고
    • ++-induced fusion and destabilization of liposomes
    • ++-induced fusion and destabilization of liposomes. Biochemistry. 24:1985;3099-3106.
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 10
    • 0032478636 scopus 로고    scopus 로고
    • Gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity
    • Eng F. J., Novikova E. G., Kuroki K., Ganem D., Fricker L. D. gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity. J. Biol. Chem. 273:1998;8382-8388.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8382-8388
    • Eng, F.J.1    Novikova, E.G.2    Kuroki, K.3    Ganem, D.4    Fricker, L.D.5
  • 12
    • 0001435504 scopus 로고    scopus 로고
    • Hepadnaviridae and their replication
    • B. N. Fields, D. M. Knipe, & P. M. Howley. Philadelphia: Lippincott-Raven
    • Ganem D. Hepadnaviridae and their replication. Fields B. N., Knipe D. M., Howley P. M. Fields Virology. 1996;2703-2737 Lippincott-Raven, Philadelphia.
    • (1996) Fields Virology , pp. 2703-2737
    • Ganem, D.1
  • 13
    • 0023080494 scopus 로고
    • The molecular biology of the hepatitis B viruses
    • Ganem D., Varmus H. E. The molecular biology of the hepatitis B viruses. Annu. Rev. Biochem. 56:1987;651-693.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 651-693
    • Ganem, D.1    Varmus, H.E.2
  • 14
    • 0027533701 scopus 로고
    • Studies of the attachment and penetration of hepatitis B virus
    • Gerlich W. H., Lu X., Heermann K. H. Studies of the attachment and penetration of hepatitis B virus. J. Hepatol. 17:1993;S10-S14.
    • (1993) J. Hepatol. , vol.17
    • Gerlich, W.H.1    Lu, X.2    Heermann, K.H.3
  • 15
    • 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., Pugh J. C. Topology of the large envelope protein of duck hepatitis B virus suggests a mechanism for membrane translocation during particle morphogenesis. J. Virol. 71:1997;1107-1114.
    • (1997) J. Virol. , vol.71 , pp. 1107-1114
    • Guo, J.-T.1    Pugh, J.C.2
  • 16
    • 0031550793 scopus 로고    scopus 로고
    • PH-independent uptake of hepatitis B virus in primary human hepatocytes
    • Hagelstein J., Fathinejad F., Stremmel W., Galle P. R. pH-independent uptake of hepatitis B virus in primary human hepatocytes. Virology. 229:1997;292-294.
    • (1997) Virology , vol.229 , pp. 292-294
    • Hagelstein, J.1    Fathinejad, F.2    Stremmel, W.3    Galle, P.R.4
  • 17
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • King D. S., Fields C. G., Fields G. B. A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis. Int. J. Peptide-Protein Res. 36:1990;255-266.
    • (1990) Int. J. Peptide-Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 18
    • 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
    • Köck J., Borst E. V., Schlicht H. I. 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. 70:1996;5827-5831.
    • (1996) J. Virol. , vol.70 , pp. 5827-5831
    • Köck, J.1    Borst, E.V.2    Schlicht, H.I.3
  • 19
    • 0028295258 scopus 로고
    • A cell surface protein that binds avian hepatitis B virus particles
    • Kuroki K., Cheung R., Marion P. L., Ganem D. A cell surface protein that binds avian hepatitis B virus particles. J. Virol. 68:1994;2091-2096.
    • (1994) J. Virol. , vol.68 , pp. 2091-2096
    • Kuroki, K.1    Cheung, R.2    Marion, P.L.3    Ganem, D.4
  • 20
    • 0029019153 scopus 로고
    • Gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family
    • Kuroki K., Eng F., Ishikawa T., Turck C., Harada F., Ganem D. gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family. J. Biol. Chem. 270:1995;15022-15028.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15022-15028
    • Kuroki, K.1    Eng, F.2    Ishikawa, T.3    Turck, C.4    Harada, F.5    Ganem, D.6
  • 22
    • 0023654706 scopus 로고
    • Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2
    • Lear J. D., DeGrado W. F. Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2. J. Biol. Chem. 262:1987;6500-6505.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6500-6505
    • Lear, J.D.1    Degrado, W.F.2
  • 23
    • 0029887665 scopus 로고    scopus 로고
    • Protease-induced infectivity of hepatitis B virus for a human hepatoblastoma cell line
    • Lu X., Block T. M., Gerlich W. H. Protease-induced infectivity of hepatitis B virus for a human hepatoblastoma cell line. J. Virol. 70:1996;2277-2285.
    • (1996) J. Virol. , vol.70 , pp. 2277-2285
    • Lu, X.1    Block, T.M.2    Gerlich, W.H.3
  • 24
    • 0028840940 scopus 로고
    • Structure and topology of the influenza virus fusion peptide in lipid bilayers
    • Lüneberg J., Martin I., Nübler F., Ruysschaert J.-M., Herrmann A. Structure and topology of the influenza virus fusion peptide in lipid bilayers. J. Biol. Chem. 270:1995;27606-27614.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27606-27614
    • Lüneberg, J.1    Martin, I.2    Nübler, F.3    Ruysschaert, J.-M.4    Herrmann, A.5
  • 25
    • 0030007530 scopus 로고    scopus 로고
    • Primary cultured normal human hepatocytes for hepatitis B virus receptor
    • Mabit H., Vons C., Dubanchet S., Capel F., Franco D., Petit M. A. Primary cultured normal human hepatocytes for hepatitis B virus receptor. J. Hepatol. 24:1996;402-412.
    • (1996) J. Hepatol. , vol.24 , pp. 402-412
    • Mabit, H.1    Vons, C.2    Dubanchet, S.3    Capel, F.4    Franco, D.5    Petit, M.A.6
  • 26
    • 0025785179 scopus 로고
    • Inhibition of duck hepatitis B virus infection with lysosomotropic agents
    • Offensperger W. B., Offensperger S., Walter E., Blum H. E., Gerok W. Inhibition of duck hepatitis B virus infection with lysosomotropic agents. Virology. 183:1991;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
  • 28
    • 0037926157 scopus 로고    scopus 로고
    • Peptides and membrane fusion: Towards an understanding of the molecular mechanism of protein-induced fusion
    • Pécheur E. I., Sainte-Marie J., Bienvenüe A., Hoekstra D. Peptides and membrane fusion: Towards an understanding of the molecular mechanism of protein-induced fusion. J. Membr. Biol. 167:1999;1-17.
    • (1999) J. Membr. Biol. , vol.167 , pp. 1-17
    • Pécheur, E.I.1    Sainte-Marie, J.2    Bienvenüe, A.3    Hoekstra, D.4
  • 29
    • 0025861478 scopus 로고
    • Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
    • Perczel A., Hollósi M., Tusnády G., Fasman G. D. Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins. Protein Eng. 4:1991;669-679.
    • (1991) Protein Eng. , vol.4 , pp. 669-679
    • Perczel, A.1    Hollósi, M.2    Tusnády, G.3    Fasman, G.D.4
  • 30
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • Rafalski M., Lear J. D., De Grado W. F. Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41. Biochemistry. 29:1990;7917-7922.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    De Grado, W.F.3
  • 31
    • 0025719093 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin: Interaction of HA2 N-terminal peptides with phospholipid vesicles
    • Rafalski M., Ortiz A., Rockwell A., van Ginkel L. C., Lear J. D., DeGrado W. F., Wilschut J. Membrane fusion activity of the influenza virus hemagglutinin: Interaction of HA2 N-terminal peptides with phospholipid vesicles. Biochemistry. 30:1991;10211-10220.
    • (1991) Biochemistry , vol.30 , pp. 10211-10220
    • Rafalski, M.1    Ortiz, A.2    Rockwell, A.3    Van Ginkel, L.C.4    Lear, J.D.5    Degrado, W.F.6    Wilschut, J.7
  • 32
    • 0026506254 scopus 로고
    • Duck hepatitis B virus infection of hepatocytes is not dependent on low pH
    • Rigg R. J., Schaller H. Duck hepatitis B virus infection of hepatocytes is not dependent on low pH. J. Virol. 66:1992;2829-2836.
    • (1992) J. Virol. , vol.66 , pp. 2829-2836
    • Rigg, R.J.1    Schaller, H.2
  • 36
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel J. J., Wiley D. C. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell. 95:1998;871-874.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 37
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor fusion
    • Struck D. K., Hoekstra D., Pagano R. E. Use of resonance energy transfer to monitor fusion. Biochemistry. 20:1981;4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 39
    • 0028856080 scopus 로고
    • Interaction between duck hepatitis B virus and a 170-kilodalton cellular protein is mediated through a neutralizing epitope of the pre-S region and occurs during viral infection
    • Tong S., Li J., Wands J. R. Interaction between duck hepatitis B virus and a 170-kilodalton cellular protein is mediated through a neutralizing epitope of the pre-S region and occurs during viral infection. J. Virol. 69:1995;7106-7112.
    • (1995) J. Virol. , vol.69 , pp. 7106-7112
    • Tong, S.1    Li, J.2    Wands, J.R.3
  • 41
    • 0022504551 scopus 로고
    • In vitro experimental infection of primary duck hepatocyte cultures with duck hepatitis B virus
    • Tuttleman J., Pugh J., Summers J. In vitro experimental infection of primary duck hepatocyte cultures with duck hepatitis B virus. J. Virol. 58:1986;17-25.
    • (1986) J. Virol. , vol.58 , pp. 17-25
    • Tuttleman, J.1    Pugh, J.2    Summers, J.3
  • 42
    • 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 K. M., 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. 72:1998;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
  • 43
    • 0025276435 scopus 로고
    • Viral and cellular fusion proteins
    • White J. M. Viral and cellular fusion proteins. Annu. Rev. Physiol. 52:1990;675-697.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-697
    • White, J.M.1
  • 44
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley D. C., Skehel J. J. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:1987;365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2


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