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Volumn 337, Issue 2, 2005, Pages 262-272

Antibody responses against wild-type yellow fever virus and the 17D vaccine strain: Characterization with human monoclonal antibody fragments and neutralization escape variants

Author keywords

Antibody response; Envelope protein; Immune library; Monoclonal antibody fragments; Neutralizing epitope; Phage display; Yellow fever virus

Indexed keywords

AMINO ACID; DIMER; EPITOPE; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS GLYCOPROTEIN; VIRUS VACCINE;

EID: 20444414884     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2005.04.031     Document Type: Article
Times cited : (44)

References (34)
  • 1
    • 0022552712 scopus 로고
    • Comparison of neurovirulence of different strains of yellow fever virus in mice
    • A.D.T. Barrett, and E.A. Gould Comparison of neurovirulence of different strains of yellow fever virus in mice J. Gen. Virol. 67 1986 631 637
    • (1986) J. Gen. Virol. , vol.67 , pp. 631-637
    • Barrett, A.D.T.1    Gould, E.A.2
  • 2
    • 0022638732 scopus 로고
    • Lethal 17D yellow fever encephalitis in mice: I. Passive protection by monoclonal antibodies to the envelope proteins of 17D yellow fever and dengue 2 viruses
    • M.W. Brandriss, J.J. Schlesinger, E.E. Walsh, and M. Briselli Lethal 17D yellow fever encephalitis in mice: I. Passive protection by monoclonal antibodies to the envelope proteins of 17D yellow fever and dengue 2 viruses J. Gen. Virol. 67 1986 229 234
    • (1986) J. Gen. Virol. , vol.67 , pp. 229-234
    • Brandriss, M.W.1    Schlesinger, J.J.2    Walsh, E.E.3    Briselli, M.4
  • 3
    • 10044263508 scopus 로고    scopus 로고
    • Localization and characterization of flavi-virus envelope glycoprotein cross-reactive epitopes
    • W.D. Crill, and G.J. Chang Localization and characterization of flavi-virus envelope glycoprotein cross-reactive epitopes J. Virol. 78 24 2004 13975 13986
    • (2004) J. Virol. , vol.78 , Issue.24 , pp. 13975-13986
    • Crill, W.D.1    Chang, G.J.2
  • 5
    • 0033199105 scopus 로고    scopus 로고
    • Molecular and biological changes associated with HeLa cell attenuation of wild-type yellow fever virus
    • L.M. Dunster, H. Wang, K.D. Ryman, B.R. Miller, S.J. Watowich, P.D. Minor, and A.D. Barrett Molecular and biological changes associated with HeLa cell attenuation of wild-type yellow fever virus Virology 261 1999 309 318
    • (1999) Virology , vol.261 , pp. 309-318
    • Dunster, L.M.1    Wang, H.2    Ryman, K.D.3    Miller, B.R.4    Watowich, S.J.5    Minor, P.D.6    Barrett, A.D.7
  • 6
    • 0021978421 scopus 로고
    • Comparative immunoelectron microscopy with monoclonal antibodies on yellow fever virus-infected cells: Pre-embedding labelling versus immunocryo-ultramicrotomy
    • H.R. Gelderblom, C. Kocks, J. L'Age-Stehr, and H. Reupke Comparative immunoelectron microscopy with monoclonal antibodies on yellow fever virus-infected cells: pre-embedding labelling versus immunocryo-ultramicrotomy J. Virol. Methods 10 1985 225 239
    • (1985) J. Virol. Methods , vol.10 , pp. 225-239
    • Gelderblom, H.R.1    Kocks, C.2    L'Age-Stehr, J.3    Reupke, H.4
  • 7
    • 8644255116 scopus 로고    scopus 로고
    • Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to the fusion loop of the dengue type 2 virus envelope glycoprotein
    • A.P. Goncalvez, R.H. Purcell, and C.-J. Lai Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to the fusion loop of the dengue type 2 virus envelope glycoprotein J. Virol. 78 2004 12919 12928
    • (2004) J. Virol. , vol.78 , pp. 12919-12928
    • Goncalvez, A.P.1    Purcell, R.H.2    Lai, C.-J.3
  • 8
    • 0022586234 scopus 로고
    • Neutralizing (54K) and nonneutralizing (54K and 48K) monoclonal antibodies against structural and non-structural yellow fever virus proteins confer immunity in mice
    • E.A. Gould, A. Buckley, A.D.T. Barrett, and N. Cammack Neutralizing (54K) and nonneutralizing (54K and 48K) monoclonal antibodies against structural and non-structural yellow fever virus proteins confer immunity in mice J. Gen. Virol. 67 1986 591 595
    • (1986) J. Gen. Virol. , vol.67 , pp. 591-595
    • Gould, E.A.1    Buckley, A.2    Barrett, A.D.T.3    Cammack, N.4
  • 9
    • 0027254174 scopus 로고
    • Comparison of the nucleotide and deduced amino acid sequences of the structural protein genes of the yellow fever 17DD vaccine strain from Senegal with those of other yellow fever vaccine viruses
    • A.D. Jennings, J.E. Whitby, P.D. Minor, and A.D. Barrett Comparison of the nucleotide and deduced amino acid sequences of the structural protein genes of the yellow fever 17DD vaccine strain from Senegal with those of other yellow fever vaccine viruses Vaccine 11 1993 679 681
    • (1993) Vaccine , vol.11 , pp. 679-681
    • Jennings, A.D.1    Whitby, J.E.2    Minor, P.D.3    Barrett, A.D.4
  • 11
    • 2442529815 scopus 로고    scopus 로고
    • Viscerotropic and neurotropic disease following vaccination with the 17D yellow fever vaccine, ARILVAX
    • S. Kitchener Viscerotropic and neurotropic disease following vaccination with the 17D yellow fever vaccine, ARILVAX Vaccine 22 2004 2103 2105
    • (2004) Vaccine , vol.22 , pp. 2103-2105
    • Kitchener, S.1
  • 12
    • 0004241743 scopus 로고    scopus 로고
    • R.E. Kontermann S. Dübel Springer Heidelberg
    • R.E. Kontermann R.E. Kontermann S. Dübel Antibody Engineering 2001 Springer Heidelberg 137 148
    • (2001) Antibody Engineering , pp. 137-148
    • Kontermann, R.E.1
  • 14
    • 10244230493 scopus 로고    scopus 로고
    • Recombinant bispecific antibodies for the targeting of adenoviruses to CEA-expressing tumour cells: A comparative analysis of bacterially expressed single-chain diabody and tandem scFv
    • T. Korn, D.M. Nettelbeck, T. Volkel, R. Muller, and R.E. Kontermann Recombinant bispecific antibodies for the targeting of adenoviruses to CEA-expressing tumour cells: a comparative analysis of bacterially expressed single-chain diabody and tandem scFv J. Gene Med. 6 2004 642 651
    • (2004) J. Gene Med. , vol.6 , pp. 642-651
    • Korn, T.1    Nettelbeck, D.M.2    Volkel, T.3    Muller, R.4    Kontermann, R.E.5
  • 16
    • 6344278186 scopus 로고    scopus 로고
    • Age-related risk of adverse events following yellow fever vaccination in Australia
    • G.L. Lawrence, M.A. Burgess, and R.B. Kass Age-related risk of adverse events following yellow fever vaccination in Australia Commun. Dis. Intell. 28 2004 244 248
    • (2004) Commun. Dis. Intell. , vol.28 , pp. 244-248
    • Lawrence, G.L.1    Burgess, M.A.2    Kass, R.B.3
  • 17
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • D.M. Knipe P.M. Howley Lippincott, Williams and Wilkins Philadelphia
    • B.D. Lindenbach, and C.M. Rice Flaviviridae: the viruses and their replication D.M. Knipe P.M. Howley Fields Virology vol. I 2001 Lippincott, Williams and Wilkins Philadelphia 991 1041
    • (2001) Fields Virology , vol.1 , pp. 991-1041
    • Lindenbach, B.D.1    Rice, C.M.2
  • 18
    • 0023577758 scopus 로고
    • Location of a neutralization determinant in the e protein of yellow fever virus (17D vaccine strain
    • M. Lobigs, L. Dalgarno, J.J. Schlesiger, and R.C. Weir Location of a neutralization determinant in the E protein of yellow fever virus (17D vaccine strain Virology 161 1987 474 478
    • (1987) Virology , vol.161 , pp. 474-478
    • Lobigs, M.1    Dalgarno, L.2    Schlesiger, J.J.3    Weir, R.C.4
  • 21
    • 0037225671 scopus 로고    scopus 로고
    • Molecular characterization of a hamster viscerotropic strain of yellow fever virus
    • M.A. McArthur, M.T. Suderman, J.P. Mutebi, S.Y. Xiao, and A.D. Barrett Molecular characterization of a hamster viscerotropic strain of yellow fever virus J. Virol. 77 2003 1462 1468
    • (2003) J. Virol. , vol.77 , pp. 1462-1468
    • McArthur, M.A.1    Suderman, M.T.2    Mutebi, J.P.3    Xiao, S.Y.4    Barrett, A.D.5
  • 22
    • 3142696041 scopus 로고    scopus 로고
    • Yellow fever vaccine
    • S.A. Plotkin W.A. Orenstein Saunders Philadelphia, USA
    • T.P. Monath Yellow fever vaccine S.A. Plotkin W.A. Orenstein Vaccines 2004 Saunders Philadelphia, USA 1095 1176
    • (2004) Vaccines , pp. 1095-1176
    • Monath, T.P.1
  • 23
    • 0642379621 scopus 로고    scopus 로고
    • Pathogenesis and pathophysiology of yellow fever
    • T.P. Monath, and A.D.T. Barrett Pathogenesis and pathophysiology of yellow fever Adv. Virus Res. 60 2003 343 395
    • (2003) Adv. Virus Res. , vol.60 , pp. 343-395
    • Monath, T.P.1    Barrett, A.D.T.2
  • 24
    • 0034947741 scopus 로고    scopus 로고
    • Phylogenetic and evolutionary relationships among yellow fever virus isolates in Africa
    • J.P. Mutebi, H.A. Wang, L. Li, and A.D. Bryant Phylogenetic and evolutionary relationships among yellow fever virus isolates in Africa J. Virol. 75 2001 6999 7008
    • (2001) J. Virol. , vol.75 , pp. 6999-7008
    • Mutebi, J.P.1    Wang, H.A.2    Li, L.3    Bryant, A.D.4
  • 25
    • 0026505138 scopus 로고
    • Recombinant vaccinia virus producing the prM and e proteins of yellow fever virus protects mice from lethal yellow fever virus encephalitis
    • S. Pincus, P.W. Mason, E. Konishi, B.A. Fonseca, R.E. Shope, C.M. Rice, and E. Paoletti Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever virus encephalitis Virology 187 1992 290 297
    • (1992) Virology , vol.187 , pp. 290-297
    • Pincus, S.1    Mason, P.W.2    Konishi, E.3    Fonseca, B.A.4    Shope, R.E.5    Rice, C.M.6    Paoletti, E.7
  • 26
    • 0026080606 scopus 로고
    • Glycosylation and secretion of yellow fever virus nonstructural protein NS1
    • P.R. Post, R. Carvalho, and R. Galler Glycosylation and secretion of yellow fever virus nonstructural protein NS1 Virus Res. 18 1991 291 302
    • (1991) Virus Res. , vol.18 , pp. 291-302
    • Post, P.R.1    Carvalho, R.2    Galler, R.3
  • 27
    • 0037081457 scopus 로고    scopus 로고
    • Heterogeneous nature of the genome of the ARILVAX yellow fever 17D vaccine revealed by consensus sequencing
    • K.V. Pugachev, S.W. Ocran, F. Guirakhoo, D. Furby, and T.P. Monath Heterogeneous nature of the genome of the ARILVAX yellow fever 17D vaccine revealed by consensus sequencing Vaccine 20 2002 996 999
    • (2002) Vaccine , vol.20 , pp. 996-999
    • Pugachev, K.V.1    Ocran, S.W.2    Guirakhoo, F.3    Furby, D.4    Monath, T.P.5
  • 28
    • 0029014434 scopus 로고
    • The envelope glycoprotein from the tick-borne encephalitis virus at 2 Å resolution
    • F.A. Rey, F.X. Heinz, C. Mandl, C. Kunz, and S.C. Harrison The envelope glycoprotein from the tick-borne encephalitis virus at 2 Å resolution Nature 375 1995 291 298
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 30
    • 1542466883 scopus 로고    scopus 로고
    • Antigenic structure of flavivirus proteins
    • J.T. Roehrig Antigenic structure of flavivirus proteins Adv. Virus Res. 59 2003 141 175
    • (2003) Adv. Virus Res. , vol.59 , pp. 141-175
    • Roehrig, J.T.1
  • 31
    • 0030979551 scopus 로고    scopus 로고
    • Yellow fever virus envelope protein has two discrete type-specific neutralizing epitopes
    • K.D. Ryman, T.N. Ledger, R.C. Weir, J.J. Schlesinger, and A.D.T. Barett Yellow fever virus envelope protein has two discrete type-specific neutralizing epitopes J. Gen. Virol. 78 1997 1352 1356
    • (1997) J. Gen. Virol. , vol.78 , pp. 1352-1356
    • Ryman, K.D.1    Ledger, T.N.2    Weir, R.C.3    Schlesinger, J.J.4    Barett, A.D.T.5
  • 32
    • 0030906211 scopus 로고    scopus 로고
    • Antigenic variants of yellow fever virus with an altered neurovirulence phenotype in mice
    • K.D. Ryman, H. Xie, T.N. Ledger, G.A. Campbell, and A.D.T. Barrett Antigenic variants of yellow fever virus with an altered neurovirulence phenotype in mice Virology 230 1997 376 380
    • (1997) Virology , vol.230 , pp. 376-380
    • Ryman, K.D.1    Xie, H.2    Ledger, T.N.3    Campbell, G.A.4    Barrett, A.D.T.5
  • 33
    • 0032565395 scopus 로고    scopus 로고
    • Mutations in a 17D-204 vaccine substrain-specific envelope protein epitope alter the pathogenesis of yellow fever virus in mice
    • K.D. Ryman, T.N. Ledger, G.A. Campbell, S.J. Watowich, and A.D.T. Barrett Mutations in a 17D-204 vaccine substrain-specific envelope protein epitope alter the pathogenesis of yellow fever virus in mice Virology 244 1998 59 65
    • (1998) Virology , vol.244 , pp. 59-65
    • Ryman, K.D.1    Ledger, T.N.2    Campbell, G.A.3    Watowich, S.J.4    Barrett, A.D.T.5


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