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Volumn 8, Issue 7, 2003, Pages 287-291

Ancient viruses in the fight against HIV

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; VIRUS FUSION PROTEIN;

EID: 0037377182     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(03)02651-5     Document Type: Note
Times cited : (2)

References (48)
  • 1
    • 0034445297 scopus 로고    scopus 로고
    • Virus membrane fusion proteins: Biological machines that undergo a metamorphosis
    • Dutch R.E., et al. Virus membrane fusion proteins: biological machines that undergo a metamorphosis. Biosci. Rep. 20:2000;597-612.
    • (2000) Biosci. Rep. , vol.20 , pp. 597-612
    • Dutch, R.E.1
  • 2
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan D.C., Kim P.S. HIV entry and its inhibition. Cell. 93:1998;681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 3
    • 0036066762 scopus 로고    scopus 로고
    • The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults
    • Kilby J.M., et al. The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults. AIDS Res. Hum. Retroviruses. 18:2002;685-693.
    • (2002) AIDS Res. Hum. Retroviruses , vol.18 , pp. 685-693
    • Kilby, J.M.1
  • 4
    • 0036090585 scopus 로고    scopus 로고
    • Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy
    • Wei X., et al. Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy. Antimicrob. Agents Chemother. 46:2002;1896-1905.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1896-1905
    • Wei, X.1
  • 5
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 angstrom resolution
    • Fass D., et al. Retrovirus envelope domain at 1.7 angstrom resolution. Nat. Struct. Biol. 3:1996;465-469.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 465-469
    • Fass, D.1
  • 6
    • 0030820095 scopus 로고    scopus 로고
    • Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution
    • Fass D., et al. Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution. Science. 277:1997;1662-1666.
    • (1997) Science , vol.277 , pp. 1662-1666
    • Fass, D.1
  • 7
    • 0018224798 scopus 로고
    • The nature of the association between the murine leukemia virus envelope proteins
    • Pinter A., et al. The nature of the association between the murine leukemia virus envelope proteins. Virology. 91:1978;345-351.
    • (1978) Virology , vol.91 , pp. 345-351
    • Pinter, A.1
  • 8
    • 0030842622 scopus 로고    scopus 로고
    • Localization of the labile disulfide bond between SU and TM of the murine leukemia virus envelope protein complex to a highly conserved CWLC motif in SU that resembles the active site sequence of thiol-disulfide exchange enzymes
    • Pinter A., et al. Localization of the labile disulfide bond between SU and TM of the murine leukemia virus envelope protein complex to a highly conserved CWLC motif in SU that resembles the active site sequence of thiol-disulfide exchange enzymes. J. Virol. 71:1997;8073-8077.
    • (1997) J. Virol. , vol.71 , pp. 8073-8077
    • Pinter, A.1
  • 9
    • 0031927203 scopus 로고    scopus 로고
    • Moloney murine leukemia virus envelope protein subunits, gp70 and Pr15E, form a stable disulfide-linked complex
    • Opstelten D.J., et al. Moloney murine leukemia virus envelope protein subunits, gp70 and Pr15E, form a stable disulfide-linked complex. J. Virol. 72:1998;6537-6545.
    • (1998) J. Virol. , vol.72 , pp. 6537-6545
    • Opstelten, D.J.1
  • 10
    • 0033658703 scopus 로고    scopus 로고
    • Sulfhydryl involvement in fusion mechanisms
    • H. Hilderson, & S. Fuller. Kluwer Academic/Plenum Publishers
    • Sanders D.A. Sulfhydryl involvement in fusion mechanisms. Hilderson H., Fuller S. Fusion of Biological Membranes and Related Problems. 2000;483-514 Kluwer Academic/Plenum Publishers.
    • (2000) Fusion of Biological Membranes and Related Problems , pp. 483-514
    • Sanders, D.A.1
  • 11
    • 0020623678 scopus 로고
    • Topography of murine leukemia virus envelope proteins: Characterization of transmembrane components
    • Pinter A., Honnen W.J. Topography of murine leukemia virus envelope proteins: characterization of transmembrane components. J. Virol. 46:1983;1056-1060.
    • (1983) J. Virol. , vol.46 , pp. 1056-1060
    • Pinter, A.1    Honnen, W.J.2
  • 12
    • 0029556891 scopus 로고
    • Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin
    • Fass D., Kim P.S. Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin. Curr. Biol. 5:1995;1377-1383.
    • (1995) Curr. Biol. , vol.5 , pp. 1377-1383
    • Fass, D.1    Kim, P.S.2
  • 13
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr C.M., Kim P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:1993;823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 14
    • 0017719251 scopus 로고
    • The presence of disulfide-linked gp70-p15(E) complexes in AKR murine leukemia virus
    • Pinter A., Fleissner E. The presence of disulfide-linked gp70-p15(E) complexes in AKR murine leukemia virus. Virology. 83:1977;417-422.
    • (1977) Virology , vol.83 , pp. 417-422
    • Pinter, A.1    Fleissner, E.2
  • 15
    • 0026325880 scopus 로고
    • Disulfide bonding controls the processing of retroviral envelope glycoproteins
    • Gliniak B.C., et al. Disulfide bonding controls the processing of retroviral envelope glycoproteins. J. Biol. Chem. 266:1991;22991-22997.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22991-22997
    • Gliniak, B.C.1
  • 16
    • 0026050289 scopus 로고
    • Cell surface sulfhydryls are required for the cytotoxicity of diphtheria toxin but not of ricin in Chinese hamster ovary cells
    • Ryser H.J., et al. Cell surface sulfhydryls are required for the cytotoxicity of diphtheria toxin but not of ricin in Chinese hamster ovary cells. J. Biol. Chem. 266:1991;18439-18442.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18439-18442
    • Ryser, H.J.1
  • 17
    • 0024337857 scopus 로고
    • Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins
    • Freedman R.B. Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell. 57:1989;1069-1072.
    • (1989) Cell , vol.57 , pp. 1069-1072
    • Freedman, R.B.1
  • 18
    • 0345772126 scopus 로고    scopus 로고
    • Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry
    • Gallina A., et al. Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry. J. Biol. Chem. 277:2002;50579-50588.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50579-50588
    • Gallina, A.1
  • 19
    • 0037474328 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CxCR4 binding and is required for fusion
    • Barbouche R., et al. Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CxCR4 binding and is required for fusion. J. Biol. Chem. 278:2003;3131-3136.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3131-3136
    • Barbouche, R.1
  • 20
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble G.W., et al. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell. 76:1994;383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1
  • 21
    • 0028865392 scopus 로고
    • GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan G.B., et al. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell Biol. 131:1995;679-691.
    • (1995) J. Cell Biol. , vol.131 , pp. 679-691
    • Melikyan, G.B.1
  • 22
    • 0027483786 scopus 로고
    • Characterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein
    • Weiss C.D., White J.M. Characterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 67:1993;7060-7066.
    • (1993) J. Virol. , vol.67 , pp. 7060-7066
    • Weiss, C.D.1    White, J.M.2
  • 23
    • 0028180109 scopus 로고
    • Uncoupled expression of Moloney murine leukemia virus envelope polypeptides SU and TM: A functional analysis of the role of TM domains in viral entry
    • Ragheb J.A., Anderson W.F. Uncoupled expression of Moloney murine leukemia virus envelope polypeptides SU and TM: a functional analysis of the role of TM domains in viral entry. J. Virol. 68:1994;3207-3219.
    • (1994) J. Virol. , vol.68 , pp. 3207-3219
    • Ragheb, J.A.1    Anderson, W.F.2
  • 24
    • 0032865298 scopus 로고    scopus 로고
    • The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion
    • Taylor G.M., Sanders D.A. The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion. Mol. Biol. Cell. 10:1999;2803-2815.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2803-2815
    • Taylor, G.M.1    Sanders, D.A.2
  • 25
    • 0033730718 scopus 로고    scopus 로고
    • A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion
    • Melikyan G.B., et al. A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion. Mol. Biol. Cell. 11:2000;3765-3775.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3765-3775
    • Melikyan, G.B.1
  • 26
    • 0035943680 scopus 로고    scopus 로고
    • Peptide mimics of the vesicular stomatitis virus G-protein transmembrane segment drive membrane fusion in vitro
    • Langosch D., et al. Peptide mimics of the vesicular stomatitis virus G-protein transmembrane segment drive membrane fusion in vitro. J. Biol. Chem. 276:2001;32016-32021.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32016-32021
    • Langosch, D.1
  • 27
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • Cleverley D.Z., Lenard J. The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein. Proc. Natl. Acad. Sci. U. S. A. 95:1998;3425-3430.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 28
    • 0029998948 scopus 로고    scopus 로고
    • Glycoprotein incorporation and HIV-1 infectivity despite exchange of the gp160 membrane-spanning domain
    • Wilk T., et al. Glycoprotein incorporation and HIV-1 infectivity despite exchange of the gp160 membrane-spanning domain. Virology. 218:1996;269-274.
    • (1996) Virology , vol.218 , pp. 269-274
    • Wilk, T.1
  • 29
    • 0017120070 scopus 로고
    • Mouse strain resistant to N-, B-, and NB-tropic murine leukemia viruses
    • Kai K., et al. Mouse strain resistant to N-, B-, and NB-tropic murine leukemia viruses. J. Virol. 20:1976;436-440.
    • (1976) J. Virol. , vol.20 , pp. 436-440
    • Kai, K.1
  • 30
    • 0019814619 scopus 로고
    • Fv-4: Gene controlling resistance to NB-tropic Friend murine leukemia virus. Distribution in wild mice, introduction into genetic background of BALB/c mice, and mapping of chromosomes
    • Odaka T., et al. Fv-4: gene controlling resistance to NB-tropic Friend murine leukemia virus. Distribution in wild mice, introduction into genetic background of BALB/c mice, and mapping of chromosomes. J. Natl. Cancer Inst. 67:1981;1123-1127.
    • (1981) J. Natl. Cancer Inst. , vol.67 , pp. 1123-1127
    • Odaka, T.1
  • 31
    • 0016790681 scopus 로고
    • FV-4: A new gene affecting the splenomegaly induction by Friend leukemia virus
    • Suzuki S. FV-4: a new gene affecting the splenomegaly induction by Friend leukemia virus. Jpn. J. Exp. Med. 45:1975;473-478.
    • (1975) Jpn. J. Exp. Med. , vol.45 , pp. 473-478
    • Suzuki, S.1
  • 32
    • 18744429635 scopus 로고    scopus 로고
    • Resistance to Friend murine leukemia virus infection conferred by the Fv-4 gene is recessive but appears dominant from the effect of the immune system
    • Zhang F., et al. Resistance to Friend murine leukemia virus infection conferred by the Fv-4 gene is recessive but appears dominant from the effect of the immune system. J. Virol. 74:2000;6193-6197.
    • (2000) J. Virol. , vol.74 , pp. 6193-6197
    • Zhang, F.1
  • 33
    • 0022183932 scopus 로고
    • Characterization of a molecularly cloned retroviral sequence associated with Fv-4 resistance
    • Ikeda H., et al. Characterization of a molecularly cloned retroviral sequence associated with Fv-4 resistance. J. Virol. 55:1985;768-777.
    • (1985) J. Virol. , vol.55 , pp. 768-777
    • Ikeda, H.1
  • 34
    • 0025261272 scopus 로고
    • Construction and characterization of the recombinant Moloney murine leukemia viruses bearing the mouse Fv-4 env gene
    • Masuda M., Yoshikura H. Construction and characterization of the recombinant Moloney murine leukemia viruses bearing the mouse Fv-4 env gene. J. Virol. 64:1990;1033-1043.
    • (1990) J. Virol. , vol.64 , pp. 1033-1043
    • Masuda, M.1    Yoshikura, H.2
  • 35
    • 0024370460 scopus 로고
    • A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection
    • Albritton L.M., et al. A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection. Cell. 57:1989;659-666.
    • (1989) Cell , vol.57 , pp. 659-666
    • Albritton, L.M.1
  • 36
    • 0027223714 scopus 로고
    • Transgenic Fv-4 mice resistant to Friend virus
    • Limjoco T.I., et al. Transgenic Fv-4 mice resistant to Friend virus. J. Virol. 67:1993;4163-4168.
    • (1993) J. Virol. , vol.67 , pp. 4163-4168
    • Limjoco, T.I.1
  • 37
    • 10544253073 scopus 로고    scopus 로고
    • Susceptibility of nude mice carrying the Fv-4 gene to Friend murine leukemia virus infection
    • Higo K., et al. Susceptibility of nude mice carrying the Fv-4 gene to Friend murine leukemia virus infection. J. Virol. 71:1997;750-754.
    • (1997) J. Virol. , vol.71 , pp. 750-754
    • Higo, K.1
  • 38
    • 0024459452 scopus 로고
    • Fv-4 resistance gene: A truncated endogenous murine leukemia virus with ecotropic interference properties
    • Ikeda H., Sugimura H. Fv-4 resistance gene: a truncated endogenous murine leukemia virus with ecotropic interference properties. J. Virol. 63:1989;5405-5412.
    • (1989) J. Virol. , vol.63 , pp. 5405-5412
    • Ikeda, H.1    Sugimura, H.2
  • 39
    • 0020546474 scopus 로고
    • Cellular expression of murine leukemia virus gp70-related antigen on thymocytes of uninfected mice correlates with Fv-4 gene-controlled resistance to Friend leukemia virus infection
    • Ikeda H., Odaka T. Cellular expression of murine leukemia virus gp70-related antigen on thymocytes of uninfected mice correlates with Fv-4 gene-controlled resistance to Friend leukemia virus infection. Virology. 128:1983;127-139.
    • (1983) Virology , vol.128 , pp. 127-139
    • Ikeda, H.1    Odaka, T.2
  • 40
    • 0034755162 scopus 로고    scopus 로고
    • Fv-4: Identification of the defect in env and the mechanism of resistance to ecotropic murine leukemia virus
    • Taylor G.M., et al. Fv-4: identification of the defect in env and the mechanism of resistance to ecotropic murine leukemia virus. J. Virol. 75:2001;11244-11248.
    • (2001) J. Virol. , vol.75 , pp. 11244-11248
    • Taylor, G.M.1
  • 41
    • 0021153680 scopus 로고
    • Different recombinant murine leukemia viruses use different cell surface receptors
    • Rein A., Schultz A. Different recombinant murine leukemia viruses use different cell surface receptors. Virology. 136:1984;144-152.
    • (1984) Virology , vol.136 , pp. 144-152
    • Rein, A.1    Schultz, A.2
  • 42
    • 0027261196 scopus 로고
    • N-linked glycosylation of the receptor for murine ecotropic retroviruses is altered in virus-infected cells
    • Kim J.W., Cunningham J.M. N-linked glycosylation of the receptor for murine ecotropic retroviruses is altered in virus-infected cells. J. Biol. Chem. 268:1993;16316-16320.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16316-16320
    • Kim, J.W.1    Cunningham, J.M.2
  • 43
    • 0035171506 scopus 로고    scopus 로고
    • A gene therapy model for retrovirus-induced disease with a viral env gene: Expression-dependent resistance in immunosuppressed hosts
    • Kitagawa M., et al. A gene therapy model for retrovirus-induced disease with a viral env gene: expression-dependent resistance in immunosuppressed hosts. Leukemia. 15:2001;1779-1784.
    • (2001) Leukemia , vol.15 , pp. 1779-1784
    • Kitagawa, M.1
  • 44
    • 0029763293 scopus 로고    scopus 로고
    • Positional cloning of the mouse retrovirus restriction gene Fv1
    • Best S., et al. Positional cloning of the mouse retrovirus restriction gene Fv1. Nature. 382:1996;826-829.
    • (1996) Nature , vol.382 , pp. 826-829
    • Best, S.1
  • 45
    • 0030588980 scopus 로고    scopus 로고
    • Single amino acid changes in the murine leukemia virus capsid protein gene define the target of Fv1 resistance
    • Kozak C.A., Chakraborti A. Single amino acid changes in the murine leukemia virus capsid protein gene define the target of Fv1 resistance. Virology. 225:1996;300-305.
    • (1996) Virology , vol.225 , pp. 300-305
    • Kozak, C.A.1    Chakraborti, A.2
  • 46
    • 0034710884 scopus 로고    scopus 로고
    • A conserved mechanism of retrovirus restriction in mammals
    • Towers G., et al. A conserved mechanism of retrovirus restriction in mammals. Proc. Natl. Acad. Sci. U. S. A. 97:2000;12295-12299.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12295-12299
    • Towers, G.1
  • 47
    • 0037015007 scopus 로고    scopus 로고
    • Cellular inhibitors with Fv1-like activity restrict human and simian immunodeficiency virus tropism
    • Cowan S., et al. Cellular inhibitors with Fv1-like activity restrict human and simian immunodeficiency virus tropism. Proc. Natl. Acad. Sci. U. S. A. 99:2002;11914-11919.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11914-11919
    • Cowan, S.1
  • 48
    • 0037015072 scopus 로고    scopus 로고
    • Restriction of lentivirus in monkeys
    • Besnier C., et al. Restriction of lentivirus in monkeys. Proc. Natl. Acad. Sci. U. S. A. 99:2002;11920-11925.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11920-11925
    • Besnier, C.1


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