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Volumn 78, Issue 3, 2004, Pages 1403-1410

The Mature Avian Leukosis Virus Subgroup A Envelope Glycoprotein Is Metastable, and Refolding Induced by the Synergistic Effects of Receptor Binding and Low pH Is Coupled to Infection

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN;

EID: 0346373694     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.3.1403-1410.2004     Document Type: Article
Times cited : (53)

References (40)
  • 1
    • 0033015821 scopus 로고    scopus 로고
    • Production and characterization of a soluble, active form of Tva, the subgroup A avian sarcoma and leukosis virus receptor
    • Balliet, J. W., J. Berson, C. M. D'Cruz, J. Huang, J. Crane, J. M. Gilbert, and P. Bates. 1999. Production and characterization of a soluble, active form of Tva, the subgroup A avian sarcoma and leukosis virus receptor. J. Virol. 73:3054-3061.
    • (1999) J. Virol. , vol.73 , pp. 3054-3061
    • Balliet, J.W.1    Berson, J.2    D'Cruz, C.M.3    Huang, J.4    Crane, J.5    Gilbert, J.M.6    Bates, P.7
  • 2
    • 0027421873 scopus 로고
    • A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor
    • Bates, P., J. A. Young, and H. E. Varmus. 1993. A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor. Cell 74:1043-1051.
    • (1993) Cell , vol.74 , pp. 1043-1051
    • Bates, P.1    Young, J.A.2    Varmus, H.E.3
  • 3
    • 0028811977 scopus 로고
    • Importance of cysteines in the LDLR-related domain of the subgroup A avian leukosis and sarcoma virus receptor for viral entry
    • Bélanger, C., K. Zingler, and J. A. T. Young. 1995. Importance of cysteines in the LDLR-related domain of the subgroup A avian leukosis and sarcoma virus receptor for viral entry. J. Virol. 69:1019-1024.
    • (1995) J. Virol. , vol.69 , pp. 1019-1024
    • Bélanger, C.1    Zingler, K.2    Young, J.A.T.3
  • 4
    • 0029780956 scopus 로고    scopus 로고
    • Protein folding and calcium binding defects arising from familial hypercholesterolemia mutations of the LDL receptor
    • Blacklow, S. C., and P. S. Kim. 1996. Protein folding and calcium binding defects arising from familial hypercholesterolemia mutations of the LDL receptor. Nat. Struct. Biol. 3:758-762.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 758-762
    • Blacklow, S.C.1    Kim, P.S.2
  • 6
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 7
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr, C. M., C. Chaudhry, and P. S. Kim. 1997. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc. Natl. Acad. Sci. USA 94:14306-14313.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 8
    • 0028324425 scopus 로고
    • A soluble form of a receptor for subgroup A avian leukosis and sarcoma viruses (ALSV-A) blocks infection and binds directly to ALSV-A
    • Connolly, L., K. Zingler, and J. A. T. Young. 1994. A soluble form of a receptor for subgroup A avian leukosis and sarcoma viruses (ALSV-A) blocks infection and binds directly to ALSV-A. J. Virol. 68:2760-2764.
    • (1994) J. Virol. , vol.68 , pp. 2760-2764
    • Connolly, L.1    Zingler, K.2    Young, J.A.T.3
  • 9
    • 0033916786 scopus 로고    scopus 로고
    • Soluble receptor-induced retroviral infection of receptor-deficient cells
    • Damico, R., and P. Bates. 2000. Soluble receptor-induced retroviral infection of receptor-deficient cells. J. Virol. 74:6469-6475.
    • (2000) J. Virol. , vol.74 , pp. 6469-6475
    • Damico, R.1    Bates, P.2
  • 10
    • 0032478191 scopus 로고    scopus 로고
    • Receptor-triggered membrane association of a model retroviral glycoprotein
    • Damico, R. L., J. Crane, and P. Bates. 1998. Receptor-triggered membrane association of a model retroviral glycoprotein. Proc. Natl. Acad. Sci. USA 95:2580-2585.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2580-2585
    • Damico, R.L.1    Crane, J.2    Bates, P.3
  • 11
    • 0036892612 scopus 로고    scopus 로고
    • Endoeytosis is a critical step in entry of subgroup B avian leukosis viruses
    • Diaz-Griffero, F., S. A. Hoschander, and J. Brojatsch. 2002. Endoeytosis is a critical step in entry of subgroup B avian leukosis viruses. J. Virol. 76:12866-12876.
    • (2002) J. Virol. , vol.76 , pp. 12866-12876
    • Diaz-Griffero, F.1    Hoschander, S.A.2    Brojatsch, J.3
  • 12
    • 0037370724 scopus 로고    scopus 로고
    • The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH
    • Earp, L. J., S. E. Delos, R. C. Netter, P. Bates, and J. M. White. 2003. The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH. J. Virol. 77:3058-3066.
    • (2003) J. Virol. , vol.77 , pp. 3058-3066
    • Earp, L.J.1    Delos, S.E.2    Netter, R.C.3    Bates, P.4    White, J.M.5
  • 13
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and P. S. Kim. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 14
    • 0030759357 scopus 로고    scopus 로고
    • Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module
    • Fass, D., S. Blacklow, P. S. Kim, and J. M. Berger. 1997. Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module. Nature 388:691-693.
    • (1997) Nature , vol.388 , pp. 691-693
    • Fass, D.1    Blacklow, S.2    Kim, P.S.3    Berger, J.M.4
  • 15
    • 0028117777 scopus 로고
    • A system for tissue-specific gene targeting: Transgcnic mice susceptible to subgroup A avian leukosis virus-based retroviral vectors
    • Federspiel, M. J., P. Bates, J. A. Young, H. E. Varmus, and S. H. Hughes. 1994. A system for tissue-specific gene targeting: transgcnic mice susceptible to subgroup A avian leukosis virus-based retroviral vectors. Proc. Natl. Acad. Sci. USA 91:11241-11245.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11241-11245
    • Federspiel, M.J.1    Bates, P.2    Young, J.A.3    Varmus, H.E.4    Hughes, S.H.5
  • 18
    • 0028146778 scopus 로고
    • The receptor for the subgroup A avian leukosis-sarcoma viruses binds to subgroup A but not to subgroup C envelope glycoprotein
    • Gilbert, J. M., P. Bates, H. E. Varmus, and J. M. White. 1994. The receptor for the subgroup A avian leukosis-sarcoma viruses binds to subgroup A but not to subgroup C envelope glycoprotein. J. Virol. 68:5623-5628.
    • (1994) J. Virol. , vol.68 , pp. 5623-5628
    • Gilbert, J.M.1    Bates, P.2    Varmus, H.E.3    White, J.M.4
  • 19
    • 0028871747 scopus 로고
    • Receptor-induced conformational changes in the subgroup A avian leukosis and sarcoma virus envelope glycoprotein
    • Gilbert, J. M., L. D. Hernandez, J. W. Balliet, P. Bates, and J. M. 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.M.1    Hernandez, L.D.2    Balliet, J.W.3    Bates, P.4    White, J.M.5
  • 20
    • 0031440116 scopus 로고    scopus 로고
    • Activation of a retroviral membrane fusion protein: Soluble receptor-induced liposome binding of the ALSV envelope glycoprotein
    • Hernandez, L. D., R. J. Peters, S. E. Delos, J. A. Young, D. A. Agard, and J. M. White. 1997. Activation of a retroviral membrane fusion protein: soluble receptor-induced liposome binding of the ALSV envelope glycoprotein. J. Cell Biol. 139:1455-1464.
    • (1997) J. Cell Biol. , vol.139 , pp. 1455-1464
    • Hernandez, L.D.1    Peters, R.J.2    Delos, S.E.3    Young, J.A.4    Agard, D.A.5    White, J.M.6
  • 21
    • 0036151820 scopus 로고    scopus 로고
    • Protonation and stability of the globular domain of influenza virus hemagglutinin
    • Huang, Q., R. Opitz, E. W. Knapp, and A. Herrmann. 2002. Protonation and stability of the globular domain of influenza virus hemagglutinin. Biophys. J. 82:1050-1058.
    • (2002) Biophys. J. , vol.82 , pp. 1050-1058
    • Huang, Q.1    Opitz, R.2    Knapp, E.W.3    Herrmann, A.4
  • 22
    • 0036091732 scopus 로고    scopus 로고
    • A fifteen-amino-acid TVB peptide serves as a minimal soluble receptor for subgroup B avian leukosis and sarcoma viruses
    • Knauss, D. J., and J. A. T. Young. 2002. A fifteen-amino-acid TVB peptide serves as a minimal soluble receptor for subgroup B avian leukosis and sarcoma viruses. J. Virol. 76:5404-5410.
    • (2002) J. Virol. , vol.76 , pp. 5404-5410
    • Knauss, D.J.1    Young, J.A.T.2
  • 23
    • 0037340005 scopus 로고    scopus 로고
    • HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation
    • Markosyan, R. M., F. S. Cohen, and G. B. Melikyan. 2003. HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation. Mol. Biol. Cell 14:926-938.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 926-938
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 24
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B., R. M. Markosyan, H. Hemmati, M. K. Delmedico, D. M. Lambert, and F. S. Cohen. 2000. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413-423.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 25
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotuin
    • Mothes, W., A. L. Boerger, S. Narayan, J. M. Cunningham, and J. A. Young. 2000. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotuin. Cell 103:679-689.
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.5
  • 26
    • 0033616638 scopus 로고    scopus 로고
    • Structural independence of ligand-binding modules five and six of the LDL receptor
    • North, C. L., and S. C. Blacklow. 1999. Structural independence of ligand-binding modules five and six of the LDL receptor. Biochemistry 38:3926-3935.
    • (1999) Biochemistry , vol.38 , pp. 3926-3935
    • North, C.L.1    Blacklow, S.C.2
  • 27
    • 0029034834 scopus 로고
    • Analysis of the subgroup A avian sarcoma and leukosis virus receptor: The 40-residue, cysteine-rich, low-density lipoprotein receptor repeat motif of Tva is sufficient to mediate viral entry
    • Rong, L., and P. Bates. 1995. Analysis of the subgroup A avian sarcoma and leukosis virus receptor: the 40-residue, cysteine-rich, low-density lipoprotein receptor repeat motif of Tva is sufficient to mediate viral entry. J. Virol. 69:4847-4853.
    • (1995) J. Virol. , vol.69 , pp. 4847-4853
    • Rong, L.1    Bates, P.2
  • 28
    • 0032555118 scopus 로고    scopus 로고
    • Conversion of a human low-density lipoprotein receptor ligand binding repeat to a virus receptor: Identification of residues important for ligand specificity
    • Rong, L., K. Gendron, and P. Bates. 1998. Conversion of a human low-density lipoprotein receptor ligand binding repeat to a virus receptor: identification of residues important for ligand specificity. Proc. Natl. Acad. Sci. USA 95:8467-8472.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8467-8472
    • Rong, L.1    Gendron, K.2    Bates, P.3
  • 29
    • 0031902358 scopus 로고    scopus 로고
    • Characterization of determinants for envelope binding and infection in Tva, the subgroup A avian sarcoma and leukosis virus receptor
    • Rong, L., K. Gendron, B. Strohl, R. Shenoy, R. J. Wool-Lewis, and P. Bates. 1998. Characterization of determinants for envelope binding and infection in Tva, the subgroup A avian sarcoma and leukosis virus receptor. J. Virol. 72:4552-4559.
    • (1998) J. Virol. , vol.72 , pp. 4552-4559
    • Rong, L.1    Gendron, K.2    Strohl, B.3    Shenoy, R.4    Wool-Lewis, R.J.5    Bates, P.6
  • 30
    • 0022886353 scopus 로고
    • Conformational changes in the hemagglutinin of influenza virus which accompany heat-induccd fusion of virus with liposomes
    • Ruigrok, R. W., S. R. Martin, S. A. Wharton, J. J. Skehel, P. M. Bayley, and D. C. Wiley. 1986. Conformational changes in the hemagglutinin of influenza virus which accompany heat-induccd fusion of virus with liposomes. Virology 155:484-497.
    • (1986) Virology , vol.155 , pp. 484-497
    • Ruigrok, R.W.1    Martin, S.R.2    Wharton, S.A.3    Skehel, J.J.4    Bayley, P.M.5    Wiley, D.C.6
  • 31
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • Russell, C. J., T. S. Jardetzky, and R. A. Lamb. 2001. Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J. 20:4024-4034.
    • (2001) EMBO J. , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 32
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J., and D. C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 33
    • 0032499531 scopus 로고    scopus 로고
    • Cell-specific viral targeting mediated by a soluble retroviral receptor-ligand fusion protein
    • Snitkovsky, S., and J. A. Young. 1998. Cell-specific viral targeting mediated by a soluble retroviral receptor-ligand fusion protein. Proc. Natl. Acad. Sci. USA 95:7063-7068.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7063-7068
    • Snitkovsky, S.1    Young, J.A.2
  • 34
    • 0035824819 scopus 로고    scopus 로고
    • The solution structure of the viral binding domain of Tva, the cellular receptor for subgroup A avian leukosis and sarcoma virus
    • Tonelli, M., R. J. Peters, T. L. James, and D. A. Agard. 2001. The solution structure of the viral binding domain of Tva, the cellular receptor for subgroup A avian leukosis and sarcoma virus. FEBS Lett. 509:161-168.
    • (2001) FEBS Lett. , vol.509 , pp. 161-168
    • Tonelli, M.1    Peters, R.J.2    James, T.L.3    Agard, D.A.4
  • 35
    • 0035133628 scopus 로고    scopus 로고
    • Role of calcium in protein folding and function of Tva, the receptor of subgroup A avian sarcoma and leukosis virus
    • Wang, Q.-Y., K. Dolmer, W. Huang, P. G. W. Gettins, and L. Rong. 2001. Role of calcium in protein folding and function of Tva, the receptor of subgroup A avian sarcoma and leukosis virus. J. Virol. 75:2051-2058.
    • (2001) J. Virol. , vol.75 , pp. 2051-2058
    • Wang, Q.-Y.1    Dolmer, K.2    Huang, W.3    Gettins, P.G.W.4    Rong, L.5
  • 36
    • 0036187925 scopus 로고    scopus 로고
    • Solution structure of the viral receptor domain of Tva and its implications in viral entry
    • Wang, Q. Y., W. Huang, K. Dolmer, P. G. Gettins, and L. Rong. 2002. Solution structure of the viral receptor domain of Tva and its implications in viral entry. J. Virol. 76:2848-2856.
    • (2002) J. Virol. , vol.76 , pp. 2848-2856
    • Wang, Q.Y.1    Huang, W.2    Dolmer, K.3    Gettins, P.G.4    Rong, L.5
  • 38
    • 0038128674 scopus 로고    scopus 로고
    • Kinetic analysis of binding interaction between the subgroup A Rous sarcoma virus glycoprotein SU and its cognate receptor Tva: Calcium is not required for ligand binding
    • Yu, X., Q. Y. Wang, Y. Gun, K. Dolmer, J. A. T. Young, P. G. W. Gettins, and L. Rong. 2003. Kinetic analysis of binding interaction between the subgroup A Rous sarcoma virus glycoprotein SU and its cognate receptor Tva: calcium is not required for ligand binding. J. Virol. 77:7517-7526.
    • (2003) J. Virol. , vol.77 , pp. 7517-7526
    • Yu, X.1    Wang, Q.Y.2    Gun, Y.3    Dolmer, K.4    Young, J.A.T.5    Gettins, P.G.W.6    Rong, L.7
  • 39
    • 0029047086 scopus 로고
    • Identification and characterization of the viral interaction determinant of the subgroup A avian leukosis virus receptor
    • Zingler, K., C. Bélanger, R. Peters, D. Agard, and J. A. T. Young. 1995. Identification and characterization of the viral interaction determinant of the subgroup A avian leukosis virus receptor. J. Virol. 69:4261-4266.
    • (1995) J. Virol. , vol.69 , pp. 4261-4266
    • Zingler, K.1    Bélanger, C.2    Peters, R.3    Agard, D.4    Young, J.A.T.5
  • 40
    • 0029816826 scopus 로고    scopus 로고
    • Residue Trp-48 of Tva is critical for viral entry but not for high-affinity binding to the SU glycoprotein of subgroup A avian leukosis and sarcoma viruses
    • Zingler, K., and J. A. Young. 1996. Residue Trp-48 of Tva is critical for viral entry but not for high-affinity binding to the SU glycoprotein of subgroup A avian leukosis and sarcoma viruses. J. Virol. 70:7510-7516.
    • (1996) J. Virol. , vol.70 , pp. 7510-7516
    • Zingler, K.1    Young, J.A.2


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