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Volumn 83, Issue 17, 2009, Pages 8575-8586

A charged second-site mutation in the fusion peptide rescues replication of a mutant avian sarcoma and leukosis virus lacking critical cysteine residues flanking the internal fusion domain

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; HYBRID PROTEIN; MUTANT PROTEIN; OLIGOMER; SERINE; VIRUS GLYCOPROTEIN; AVIAN PROTEIN; TVA RECEPTOR; VIRUS FUSION PROTEIN; VIRUS RECEPTOR;

EID: 69249218002     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00526-09     Document Type: Article
Times cited : (5)

References (36)
  • 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
    • 29144449872 scopus 로고    scopus 로고
    • Avian sarcoma and leukosis virus-receptor interactions: From classical genetics to novel insights into virus-cell membrane fusion
    • Barnard, R. J., D. Elleder, and J. A. T. Young. 2006. Avian sarcoma and leukosis virus-receptor interactions: from classical genetics to novel insights into virus-cell membrane fusion. Virology 344:25-29.
    • (2006) Virology , vol.344 , pp. 25-29
    • Barnard, R.J.1    Elleder, D.2    Young, J.A.T.3
  • 4
    • 11244258848 scopus 로고    scopus 로고
    • Structure and membrane interaction of the internal fusion peptide of avian sarcoma and leukosis virus
    • Cheng, S.-F., C.-W. Wu, E. A. B. Kantchev, and D.-K. Chang. 2004. Structure and membrane interaction of the internal fusion peptide of avian sarcoma and leukosis virus. Eur. J. Biochem. 271:4725-4736.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4725-4736
    • Cheng, S.-F.1    Wu, C.-W.2    Kantchev, E.A.B.3    Chang, D.-K.4
  • 5
    • 0033015740 scopus 로고    scopus 로고
    • Substitutions in the receptor-binding domain of the avian sarcoma and leukosis virus envelope uncouple receptor-triggered structural rearrangements in the surface and transmembrane subunits
    • Damico, R., L. Rong, and P. Bates. 1999. Substitutions in the receptor-binding domain of the avian sarcoma and leukosis virus envelope uncouple receptor-triggered structural rearrangements in the surface and transmembrane subunits. J. Virol. 73:3087-3094. (Pubitemid 29135698)
    • (1999) Journal of Virology , vol.73 , Issue.4 , pp. 3087-3094
    • Damico, R.1    Rong, L.2    Bates, P.3
  • 6
    • 40149083415 scopus 로고    scopus 로고
    • Cysteines flanking the internal fusion peptide are required for the avian sarcoma/leukosis virus glycoprotein to mediate the lipid mixing stage of fusion with high efficiency
    • Delos, S. E., M. B. Brecher, Z. Chen, D. C. Melder, M. J. Federspiel, and J. M. White. 2008. Cysteines flanking the internal fusion peptide are required for the avian sarcoma/leukosis virus glycoprotein to mediate the lipid mixing stage of fusion with high efficiency. J. Virol. 82:3131-3134.
    • (2008) J. Virol. , vol.82 , pp. 3131-3134
    • Delos, S.E.1    Brecher, M.B.2    Chen, Z.3    Melder, D.C.4    Federspiel, M.J.5    White, J.M.6
  • 7
    • 0033947260 scopus 로고    scopus 로고
    • The central proline of an internal viral fusion peptide serves two important roles
    • Delos, S. E., J. M. Gilbert, and J. M. White. 2000. The central proline of an internal viral fusion peptide serves two important roles. J. Virol. 74:1686-1693.
    • (2000) J. Virol. , vol.74 , pp. 1686-1693
    • Delos, S.E.1    Gilbert, J.M.2    White, J.M.3
  • 8
    • 0033809570 scopus 로고    scopus 로고
    • Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leukosis virus envelope glycoprotein
    • Delos, S. E., and J. M. White. 2000. Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leukosis virus envelope glycoprotein. J. Virol. 74:9738-9741.
    • (2000) J. Virol. , vol.74 , pp. 9738-9741
    • Delos, S.E.1    White, J.M.2
  • 10
    • 0030591276 scopus 로고    scopus 로고
    • Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses
    • Gallaher, W. R. 1996. Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses. Cell 85:477-478.
    • (1996) Cell , vol.85 , pp. 477-478
    • Gallaher, W.R.1
  • 11
    • 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
  • 12
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change in the fusion domain from influenza hemagglutinin
    • Han, X., J. H. Bushweller, D. S. Cafiso, and L. K. Tamm. 2001. Membrane structure and fusion-triggering conformational change in the fusion domain from influenza hemagglutinin. Nat. Struct. Biol. 8:715-720.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 14
    • 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. T. 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.T.4    Agard, D.A.5    White, J.M.6
  • 15
    • 0032169950 scopus 로고    scopus 로고
    • The DF-1 chicken fibroblast cell line: Transformation induced by diverse oncogenes and cell death resulting from infection by avian leukosis viruses
    • DOI 10.1006/viro.1998.9290
    • Himly, M., D. N. Foster, I. Bottoli, J. S. Iacovoni, and P. K. Vogt. 1998. The DF-1 chicken fibroblast cell line: transformation induced by diverse oncogenes and cell death resulting from infection by avian leukosis viruses. Virology 248:295-304. (Pubitemid 28417716)
    • (1998) Virology , vol.248 , Issue.2 , pp. 295-304
    • Himly, M.1    Foster, D.N.2    Bottoli, I.3    Iacovoni, J.S.4    Vogt, P.K.5
  • 16
    • 0035158622 scopus 로고    scopus 로고
    • Identification of key residues in subgroup a avian leukosis virus envelope determining receptor binding affinity and infectivity of cells expressing chicken or quail Tva receptor
    • Holmen, S. L., D. C. Melder, and M. J. Federspiel. 2001. Identification of key residues in subgroup A avian leukosis virus envelope determining receptor binding affinity and infectivity of cells expressing chicken or quail Tva receptor. J. Virol. 75:726-737.
    • (2001) J. Virol. , vol.75 , pp. 726-737
    • Holmen, S.L.1    Melder, D.C.2    Federspiel, M.J.3
  • 17
    • 0032731095 scopus 로고    scopus 로고
    • Soluble forms of the subgroup a avian leukosis virus [ALV(A)] receptor Tva significantly inhibit ALV(A) infection in vitro and in vivo
    • Holmen, S. L., D. W. Salter, W. S. Payne, J. B. Dodgson, S. H. Hughes, and M. J. Federspiel. 1999. Soluble forms of the subgroup A avian leukosis virus [ALV(A)] receptor Tva significantly inhibit ALV(A) infection in vitro and in vivo. J. Virol. 73:10051-10060.
    • (1999) J. Virol. , vol.73 , pp. 10051-10060
    • Holmen, S.L.1    Salter, D.W.2    Payne, W.S.3    Dodgson, J.B.4    Hughes, S.H.5    Federspiel, M.J.6
  • 18
    • 0002614837 scopus 로고    scopus 로고
    • Viral entry and receptors
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hunter, E. 1997. Viral entry and receptors, p. 71-120. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1997) Retroviruses , pp. 71-120
    • Hunter, E.1
  • 19
    • 0032849336 scopus 로고    scopus 로고
    • Mutational analysis of the putative fusion domain of Ebola virus glycoprotein
    • Ito, H., S. Watanabe, A. Sanchez, M. A. Whitt, and Y. Kawaoka. 1999. Mutational analysis of the putative fusion domain of Ebola virus glycoprotein. J. Virol. 73:8907-8912. (Pubitemid 29441763)
    • (1999) Journal of Virology , vol.73 , Issue.10 , pp. 8907-8912
    • Ito, H.1    Watanabe, S.2    Sanchez, A.3    Whitt, M.A.4    Kawaoka, Y.5
  • 20
    • 0036893140 scopus 로고    scopus 로고
    • Covalent modifications of the Ebola virus glycoprotein
    • Jeffers, S. A., D. A. Sanders, and A. Sanchez. 2002. Covalent modifications of the Ebola virus glycoprotein. J. Virol. 76:12463-12472.
    • (2002) J. Virol. , vol.76 , pp. 12463-12472
    • Jeffers, S.A.1    Sanders, D.A.2    Sanchez, A.3
  • 21
    • 0000704627 scopus 로고
    • Introduction of DNA into eukaryotic cells
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), John Wiley & Sons, Inc., New York, NY
    • Kingston, R. E., C. A. Chen, and H. Okayama. 1989. Introduction of DNA into eukaryotic cells, p. 911-919. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol.1. John Wiley & Sons, Inc., New York, NY.
    • (1989) Current Protocols in Molecular Biology , vol.1 , pp. 911-919
    • Kingston, R.E.1    Chen, C.A.2    Okayama, H.3
  • 22
    • 16344374327 scopus 로고    scopus 로고
    • A study of low pH-induced refolding of Env of avian sarcoma and leukosis virus into a six-helix bundle
    • Markosyan, R. M., P. Bates, F. S. Cohen, and G. B. Melikyan. 2004. A study of low pH-induced refolding of Env of avian sarcoma and leukosis virus into a six-helix bundle. Biophys. J. 87:3291-3298.
    • (2004) Biophys. J. , vol.87 , pp. 3291-3298
    • Markosyan, R.M.1    Bates, P.2    Cohen, F.S.3    Melikyan, G.B.4
  • 23
    • 3242713988 scopus 로고    scopus 로고
    • Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein
    • DOI 10.1128/JVI.78.15.8201-8209.2004
    • Matsuyama, S., S. E. Delos, and J. M. White. 2004. Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein. J. Virol. 78:8201-8209. (Pubitemid 38944303)
    • (2004) Journal of Virology , vol.78 , Issue.15 , pp. 8201-8209
    • Matsuyama, S.1    Delos, S.E.2    White, J.M.3
  • 25
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes, W., A. L. Boerger, S. Narayan, J. M. Cunningham, and J. A. T. Young. 2000. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 103:679-689. (Pubitemid 30954010)
    • (2000) Cell , vol.103 , Issue.4 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.T.5
  • 26
    • 10044241596 scopus 로고    scopus 로고
    • Heptad repeat 2-based peptides inhibit avian sarcoma and leukosis virus subgroup a infection and identify a fusion intermediate
    • Netter, R. C., S. M. Amberg, J. W. Balliet, M. J. Biscone, A. Vermeulen, L. J. Earp, J. M. White, and P. Bates. 2004. Heptad repeat 2-based peptides inhibit avian sarcoma and leukosis virus subgroup A infection and identify a fusion intermediate. J. Virol. 78:13430-13439.
    • (2004) J. Virol. , vol.78 , pp. 13430-13439
    • Netter, R.C.1    Amberg, S.M.2    Balliet, J.W.3    Biscone, M.J.4    Vermeulen, A.5    Earp, L.J.6    White, J.M.7    Bates, P.8
  • 27
    • 0038487379 scopus 로고    scopus 로고
    • Are fusion peptides a good model to study viral cell fusion?
    • Nieva, J. L., and A. Agirre. 2003. Are fusion peptides a good model to study viral cell fusion? Biochim. Biophys. Acta 1614:104-115.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 104-115
    • Nieva, J.L.1    Agirre, A.2
  • 28
    • 0036310245 scopus 로고    scopus 로고
    • Novel monoclonal antibody directed at the receptor binding site on the avian sarcoma and leukosis virus Env complex
    • DOI 10.1128/JVI.76.15.7518-7527.2002
    • Ochsenbauer-Jambor, C., S. E. Delos, M. A. Accavitti, J. M. White, and E. Hunter. 2002. Novel monoclonal antibody directed at the receptor binding site on the avian sarcoma and leukosis virus Env complex. J. Virol. 76:7518-7527. (Pubitemid 34760974)
    • (2002) Journal of Virology , vol.76 , Issue.15 , pp. 7518-7527
    • Ochsenbauer-Jambor, C.1    Delos, S.E.2    Accavitti, M.A.3    White, J.M.4    Hunter, E.5
  • 29
    • 0032168060 scopus 로고    scopus 로고
    • The EV-O-derived cell line DF-1 supports the efficient replication of avian leukosis-sarcoma viruses and vectors
    • DOI 10.1006/viro.1998.9291
    • Schaefer-Klein, J., I. Givol, E. V. Barsov, J. M. Whitcomb, M. VanBrocklin, D. N. Foster, M. J. Federspiel, and S. H. Hughes. 1998. The EV-0-derived cell line DF-1 supports efficient replication of avian leukosis-sarcoma viruses and vectors. Virology 248:305-311. (Pubitemid 28417717)
    • (1998) Virology , vol.248 , Issue.2 , pp. 305-311
    • Schaefer-Klein, J.1    Givol, I.2    Barsov, E.V.3    Whitcomb, J.M.4    Vanbrocklin, M.5    Foster, D.N.6    Federspiel, M.J.7    Hughes, S.H.8
  • 30
    • 0018489146 scopus 로고
    • An enzyme-linked immunoabsorbant assay for detecting avian leukosis sarcoma viruses
    • Smith, E. J., A. M. Fadly, and W. Okazaki. 1979. An enzyme-linked immunoabsorbant assay for detecting avian leukosis sarcoma viruses. Avian Dis. 23:698-707.
    • (1979) Avian Dis. , vol.23 , pp. 698-707
    • Smith, E.J.1    Fadly, A.M.2    Okazaki, W.3
  • 31
    • 0346373694 scopus 로고    scopus 로고
    • 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
    • Smith, J. G., W. Mothes, S. C. Blacklow, and J. M. Cunningham. 2004. 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. J. Virol. 78:1403-1410.
    • (2004) J. Virol. , vol.78 , pp. 1403-1410
    • Smith, J.G.1    Mothes, W.2    Blacklow, S.C.3    Cunningham, J.M.4
  • 32
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Swanstrom, R., and J. W. Wills. 1997. Synthesis, assembly, and processing of viral proteins, p. 263-334. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 33
    • 0038825375 scopus 로고    scopus 로고
    • Hypothesis: Spring-loaded boomerang mechanism of influenza virus hemagglutinin-mediated membrane fusion
    • Tamm, L. K. 2003. Hypothesis: spring-loaded boomerang mechanism of influenza virus hemagglutinin-mediated membrane fusion. Biochim. Biophys. Acta 1614:14-23.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 14-23
    • Tamm, L.K.1
  • 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
    • DOI 10.1016/S0014-5793(01)03086-1, PII S0014579301030861
    • 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. (Pubitemid 34015935)
    • (2001) FEBS Letters , vol.509 , Issue.2 , pp. 161-168
    • Tonelli, M.1    Peters, R.J.2    James, T.L.3    Agard, D.A.4
  • 35
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • White, J. M., S. E. Delos, M. Brecher, and K. Schornberg. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 36
    • 0037740342 scopus 로고    scopus 로고
    • Virus entry and uncoating
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Lippincott Williams & Wilkins, Philadelphia, PA
    • Young, J. A. T. 2001. Virus entry and uncoating., p. 87-103. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 4th ed., vol.2. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2001) Fields Virology, 4th Ed. , vol.2 , pp. 87-103
    • Young, J.A.T.1


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