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Volumn 78, Issue 10, 1997, Pages 2431-2439

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; VIRUS ANTIBODY;

EID: 0030732117     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/0022-1317-78-10-2431     Document Type: Article
Times cited : (30)

References (30)
  • 2
    • 0028329180 scopus 로고
    • Effect of antibody valency on interaction with cell-surface expressed HIV-1 and viral neutralization
    • Cavacini, L. A., Emes, C. L., Power, J., Duval, M. & Posner, M. R. (1994). Effect of antibody valency on interaction with cell-surface expressed HIV-1 and viral neutralization. Journal of Immunology 152, 2538-2545.
    • (1994) Journal of Immunology , vol.152 , pp. 2538-2545
    • Cavacini, L.A.1    Emes, C.L.2    Power, J.3    Duval, M.4    Posner, M.R.5
  • 6
    • 0029552239 scopus 로고
    • Update on the neutralisation of animal viruses
    • Dimmock, N. J. (1995). Update on the neutralisation of animal viruses. Reviews in Medical Virology 5, 165-179.
    • (1995) Reviews in Medical Virology , vol.5 , pp. 165-179
    • Dimmock, N.J.1
  • 7
    • 0016240079 scopus 로고
    • Antibody affinity. VI. Synthesis of bivalent lactosyl haptens and their interaction with anti-lactosyl antibodies
    • Gopalakrishnan, P. V. & Karush, F. (1974). Antibody affinity. VI. Synthesis of bivalent lactosyl haptens and their interaction with anti-lactosyl antibodies. Immunochemistry 11, 279-283.
    • (1974) Immunochemistry , vol.11 , pp. 279-283
    • Gopalakrishnan, P.V.1    Karush, F.2
  • 8
    • 0016139612 scopus 로고
    • Fowl plague virus replication in mammalian cell-erythrocyte heterokaryons: Studies concerning the actinomycin D and ultra-violet sensitive phase in influenza virus replication
    • Kelly, D. C. & Dimmock, N. J. (1974). Fowl plague virus replication in mammalian cell-erythrocyte heterokaryons: studies concerning the actinomycin D and ultra-violet sensitive phase in influenza virus replication. Virology 61, 210-222.
    • (1974) Virology , vol.61 , pp. 210-222
    • Kelly, D.C.1    Dimmock, N.J.2
  • 9
    • 0022117016 scopus 로고
    • Interference with a conformational change in the HA molecule of influenza virus by antibodies as a possible neutralization mechanism
    • Kida, H., Yoden, S., Kuwabara, M. & Yanagawa, R. (1985). Interference with a conformational change in the HA molecule of influenza virus by antibodies as a possible neutralization mechanism. Vaccine 3, 219-222.
    • (1985) Vaccine , vol.3 , pp. 219-222
    • Kida, H.1    Yoden, S.2    Kuwabara, M.3    Yanagawa, R.4
  • 10
    • 0025967904 scopus 로고
    • Effects of specific monoclonal antibodies on La Crosse virus neutralization: Aggregation, inactivation by Fab fragments, and inhibition of attachment to baby hamster kidney cells
    • Kingsford, L., Boucquey, K. H. & Cardoso, T. P. (1991). Effects of specific monoclonal antibodies on La Crosse virus neutralization: aggregation, inactivation by Fab fragments, and inhibition of attachment to baby hamster kidney cells. Virology 180, 591-601.
    • (1991) Virology , vol.180 , pp. 591-601
    • Kingsford, L.1    Boucquey, K.H.2    Cardoso, T.P.3
  • 11
    • 0003071978 scopus 로고
    • The interaction between virus and antibody. II. Mechanism of the reaction
    • Lafferty, K. J. (1963). The interaction between virus and antibody. II. Mechanism of the reaction. Virology 21, 76-90.
    • (1963) Virology , vol.21 , pp. 76-90
    • Lafferty, K.J.1
  • 12
    • 0028957940 scopus 로고
    • Protection from lethal coronavirus infection by immunoglobulin fragments
    • Lamarre, A. & Talbot, P. J. (1995). Protection from lethal coronavirus infection by immunoglobulin fragments. Journal of Immunology 154, 3975-3984.
    • (1995) Journal of Immunology , vol.154 , pp. 3975-3984
    • Lamarre, A.1    Talbot, P.J.2
  • 13
    • 0030850077 scopus 로고    scopus 로고
    • A human IgG1 (b12) specific for the CD4 binding site of HIV-1 neutralizes by inhibiting the virus fusion entry process, but b12 Fab neutralizes by inhibiting a post-fusion event
    • McInerney, T. L., McLain, L., Armstrong, S. J. & Dimmock, N. J. (1997). A human IgG1 (b12) specific for the CD4 binding site of HIV-1 neutralizes by inhibiting the virus fusion entry process, but b12 Fab neutralizes by inhibiting a post-fusion event. Virology 233, 313-326.
    • (1997) Virology , vol.233 , pp. 313-326
    • McInerney, T.L.1    McLain, L.2    Armstrong, S.J.3    Dimmock, N.J.4
  • 14
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D. & Ehrhardt, W. (1988). Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 15
    • 0004070428 scopus 로고
    • 5. The three-dimensional structure of immunoglobulins
    • Edited by A. Nisonoff, J. E. Hopper & S. B. Spring. New York: Academic Press
    • Nisonoff, A., Hopper, J. E. & Spring, S. B. (1975). 5. The three-dimensional structure of immunoglobulins. In The Antibody Molecule, pp. 209-237. Edited by A. Nisonoff, J. E. Hopper & S. B. Spring. New York: Academic Press.
    • (1975) The Antibody Molecule , pp. 209-237
    • Nisonoff, A.1    Hopper, J.E.2    Spring, S.B.3
  • 16
    • 0025008801 scopus 로고
    • Mechanisms of neutralization of influenza virus on mouse tracheal epithelial cells by mouse monoclonal polymeric IgA and polyclonal IgM directed against the viral haemagglutinin
    • Outlaw, M. C. & Dimmock, N. J. (1990). Mechanisms of neutralization of influenza virus on mouse tracheal epithelial cells by mouse monoclonal polymeric IgA and polyclonal IgM directed against the viral haemagglutinin. Journal of General Virology 71, 69-76.
    • (1990) Journal of General Virology , vol.71 , pp. 69-76
    • Outlaw, M.C.1    Dimmock, N.J.2
  • 17
    • 0025114153 scopus 로고
    • Mechanisms of neutralization of influenza virus vary according to IgG concentration
    • Outlaw, M. C., Armstrong, S. J. & Dimmock, N. J. (1990). Mechanisms of neutralization of influenza virus vary according to IgG concentration. Virology 178, 478-485.
    • (1990) Virology , vol.178 , pp. 478-485
    • Outlaw, M.C.1    Armstrong, S.J.2    Dimmock, N.J.3
  • 18
    • 0027974229 scopus 로고
    • Direct imaging of interactions between an icosahedral virus and conjugate fragments by cryoelectron microscopy and X-ray crystallography
    • Porta, C., Wang, G., Cheng, H., Chen, Z., Baker, T. S. & Johnson, J. E. (1994). Direct imaging of interactions between an icosahedral virus and conjugate fragments by cryoelectron microscopy and X-ray crystallography. Virology 204, 777-778.
    • (1994) Virology , vol.204 , pp. 777-778
    • Porta, C.1    Wang, G.2    Cheng, H.3    Chen, Z.4    Baker, T.S.5    Johnson, J.E.6
  • 19
    • 0028291731 scopus 로고
    • Recognition of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1
    • Roben, P., Moore, J. P., Sodroski, J., Barbas, C. F., III & Burton, D. R. (1994). Recognition of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. Journal of Virology 68, 4821-4828.
    • (1994) Journal of Virology , vol.68 , pp. 4821-4828
    • Roben, P.1    Moore, J.P.2    Sodroski, J.3    Barbas III, C.F.4    Burton, D.R.5
  • 20
    • 0030272911 scopus 로고    scopus 로고
    • Determination of affinities of a panel of IgGs and Fabs for an enveloped (influenza A) virus using surface plasmon resonance
    • Schofield, D. J. & Dimmock, N. J. (1996). Determination of affinities of a panel of IgGs and Fabs for an enveloped (influenza A) virus using surface plasmon resonance. Journal of Virological Methods 62, 33-42.
    • (1996) Journal of Virological Methods , vol.62 , pp. 33-42
    • Schofield, D.J.1    Dimmock, N.J.2
  • 21
    • 0030815421 scopus 로고    scopus 로고
    • High and low efficiency neutralization epitopes on the haemagglutinin of type A influenza virus
    • Schofield, D. J., Stephenson, J. R. & Dimmock, N. J. (1997). High and low efficiency neutralization epitopes on the haemagglutinin of type A influenza virus. Journal of General Virology 78, 2441-2446.
    • (1997) Journal of General Virology , vol.78 , pp. 2441-2446
    • Schofield, D.J.1    Stephenson, J.R.2    Dimmock, N.J.3
  • 23
    • 0000996032 scopus 로고    scopus 로고
    • Antibody-mediated neutralization of picomaviruses
    • Edited by W. Chin, R. M. Burnett & R. L. Garcea. New York: Oxford Press
    • Smith, T. J. & Mosser, A. G. (1996). Antibody-mediated neutralization of picomaviruses. In Structural Biology of Viruses, pp. 134-156. Edited by W. Chin, R. M. Burnett & R. L. Garcea. New York: Oxford Press.
    • (1996) Structural Biology of Viruses , pp. 134-156
    • Smith, T.J.1    Mosser, A.G.2
  • 25
    • 0022049447 scopus 로고
    • A monoclonal antibody that neutralizes poliovirus by crosslinking virions
    • Thomas, A. D. M., Brioen, P. & Boeyé, A. (1985). A monoclonal antibody that neutralizes poliovirus by crosslinking virions. Journal of Virology 54, 7-13.
    • (1985) Journal of Virology , vol.54 , pp. 7-13
    • Thomas, A.D.M.1    Brioen, P.2    Boeyé, A.3
  • 26
    • 0014202658 scopus 로고
    • Electron microscopy of an antibody-hapten complex
    • Valentine, R. C. & Green, N. M. (1967). Electron microscopy of an antibody-hapten complex. Journal of Molecular Biology 27, 615-617.
    • (1967) Journal of Molecular Biology , vol.27 , pp. 615-617
    • Valentine, R.C.1    Green, N.M.2
  • 28
    • 0002865114 scopus 로고
    • Structure, function and antigenicity of the hemagglutinin of influenza virus
    • Edited by R. M. Krug. New York: Plenum Press
    • Wharton, S. A., Weis, W., Skehel, J. J. & Wiley, D. C. (1989). Structure, function and antigenicity of the hemagglutinin of influenza virus. In The Influenza Viruses, pp. 153-173. Edited by R. M. Krug. New York: Plenum Press.
    • (1989) The Influenza Viruses , pp. 153-173
    • Wharton, S.A.1    Weis, W.2    Skehel, J.J.3    Wiley, D.C.4
  • 29
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • Wiley, D. C., Wilson, I. A. & Skehel, J. J. (1981). Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289, 373-378.
    • (1981) Nature , vol.289 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 30
    • 0021855692 scopus 로고
    • Is bivalent binding of monoclonal antibodies to different antigenic areas on the hemagglutinin of influenza virus required for neutralization of viral infectivity?
    • Yoden, S., Kida, H. & Yanagawa, R. (1985). Is bivalent binding of monoclonal antibodies to different antigenic areas on the hemagglutinin of influenza virus required for neutralization of viral infectivity? Archives of Virology 85, 209-216.
    • (1985) Archives of Virology , vol.85 , pp. 209-216
    • Yoden, S.1    Kida, H.2    Yanagawa, R.3


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