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Volumn 62, Issue 1, 1996, Pages 33-42

Determination of affinities of a panel of IgGs and Fabs for whole enveloped (influenza A) virions using surface plasmon resonance

Author keywords

affinity; Fab; IgG; influenza A virus; surface plasmon resonance

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY;

EID: 0030272911     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/0166-0934(96)02086-1     Document Type: Article
Times cited : (52)

References (41)
  • 1
    • 0028348564 scopus 로고
    • In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain specificity
    • Barbas III, C.F., Hu, D., Dunlop, N. et al. (1994) In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain specificity. Proc. Natl. Acad. Sci. USA 91, 3809-3813.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3809-3813
    • Barbas C.F. III1    Hu, D.2    Dunlop, N.3
  • 2
    • 0026486724 scopus 로고
    • Human monoclonal Fab fragments derived from a combinatorial library bind to respiratory syncytial virus F glycoprotein and neutralizes infectivity
    • Barbas III, C.F., Crowe, J.E., Cababa, D. et al. (1992) Human monoclonal Fab fragments derived from a combinatorial library bind to respiratory syncytial virus F glycoprotein and neutralizes infectivity. Proc. Natl. Acad. Sci. USA 89, 10164-10168.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10164-10168
    • Barbas C.F. III1    Crowe, J.E.2    Cababa, D.3
  • 3
    • 0015307141 scopus 로고
    • Antibody affinity and valence in viral neutralization
    • Blank, S.E., Leslie, G.A. and Clem, L.W. (1972) Antibody affinity and valence in viral neutralization. J. Immunol. 108, 665-673.
    • (1972) J. Immunol. , vol.108 , pp. 665-673
    • Blank, S.E.1    Leslie, G.A.2    Clem, L.W.3
  • 4
    • 0026768221 scopus 로고
    • Detection of receptor-ligand interaction using surface plasmon resonance: Model studies employing the HIV-1 gp120/CD4 interaction
    • Brigham-Burke, M., Edwards, J.R. and O'Shannessy, D.J. (1992) Detection of receptor-ligand interaction using surface plasmon resonance: model studies employing the HIV-1 gp120/CD4 interaction. Anal. Biochem. 205, 125-131.
    • (1992) Anal. Biochem. , vol.205 , pp. 125-131
    • Brigham-Burke, M.1    Edwards, J.R.2    O'Shannessy, D.J.3
  • 5
    • 0027985431 scopus 로고
    • Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody
    • Burton, D.R., Pyati, J., Koduri, R. et al. (1994) Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 266, 1024-1027.
    • (1994) Science , vol.266 , pp. 1024-1027
    • Burton, D.R.1    Pyati, J.2    Koduri, R.3
  • 6
    • 0029063466 scopus 로고
    • Kinetics and thermodynamics of virus binding to receptor: Studies with rhinovirus, intracellular adhesion molecule-1 (ICAM-1) and surface plasmon resonance
    • Casasnovas, J.M. and Springer, T.A. (1995) Kinetics and thermodynamics of virus binding to receptor: Studies with rhinovirus, intracellular adhesion molecule-1 (ICAM-1) and surface plasmon resonance. J. Biol. Chem. 270, 13216-13224.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13216-13224
    • Casasnovas, J.M.1    Springer, T.A.2
  • 7
    • 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. and Posner, M.R. (1994) Effect of antibody valency on interaction with cell-surface expressed HIV-1 and viral neutralization. J. Immunol. 152, 2538-2545.
    • (1994) J. Immunol. , vol.152 , pp. 2538-2545
    • Cavacini, L.A.1    Emes, C.L.2    Power, J.3    Duval, M.4    Posner, M.R.5
  • 8
    • 0028208268 scopus 로고
    • Neutralization of divergent human immunodeficiency virus type 1 variants and primary isolates by IAM-42-2F5, an anti-gp41 human monoclonal antibody
    • Conley, A.J., Kessler, II J.A., Boots, L.J. et al. (1994) Neutralization of divergent human immunodeficiency virus type 1 variants and primary isolates by IAM-42-2F5, an anti-gp41 human monoclonal antibody. Proc. Natl. Acad. Sci. USA 91, 3348-3352.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3348-3352
    • Conley, A.J.1    Kessler J.A. II2    Boots, L.J.3
  • 9
    • 0028831142 scopus 로고
    • Neutralizing recombinant human antibodies to a conformational V2-and CD4 binding site-sensitive epitope of HIV-1 gp120 isolated using an epitope masking procedure
    • Ditzel, H.D., Binley, J.M., Moore, J.P. et al. (1995) Neutralizing recombinant human antibodies to a conformational V2-and CD4 binding site-sensitive epitope of HIV-1 gp120 isolated using an epitope masking procedure. J. Immunol. 154, 895-908.
    • (1995) J. Immunol. , vol.154 , pp. 895-908
    • Ditzel, H.D.1    Binley, J.M.2    Moore, J.P.3
  • 10
    • 0026568808 scopus 로고
    • Mapping of viral epitopes with conformationally specific monoclonal antibodies using biosensor technology
    • Dubs, M.C., Altschuh, D. and Van Regenmortel, M.H.V. (1992) Mapping of viral epitopes with conformationally specific monoclonal antibodies using biosensor technology. J. Chromatogr. 597, 391-396.
    • (1992) J. Chromatogr. , vol.597 , pp. 391-396
    • Dubs, M.C.1    Altschuh, D.2    Van Regenmortel, M.H.V.3
  • 11
    • 0026799533 scopus 로고
    • Interaction between viruses and monoclonal antibodies studied by surface plasmon resonance
    • Dubs, M.C., Altschuh, D. and Van Regenmortel, M.H.V. (1991) Interaction between viruses and monoclonal antibodies studied by surface plasmon resonance. Immunol. Letts. 31, 59-64.
    • (1991) Immunol. Letts. , vol.31 , pp. 59-64
    • Dubs, M.C.1    Altschuh, D.2    Van Regenmortel, M.H.V.3
  • 12
    • 0027971620 scopus 로고
    • Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein
    • Godet, M., Grosclaude, J., Delmas, B. and Laude, H. (1994) Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein. J. Virol. 68, 8008-8016.
    • (1994) J. Virol. , vol.68 , pp. 8008-8016
    • Godet, M.1    Grosclaude, J.2    Delmas, B.3    Laude, H.4
  • 13
    • 0027473684 scopus 로고
    • Human anti-self antibodies with high specificity from phage display libraries
    • Griffiths, A.D., Malmqvist, M., Marks, J.D. et al. (1993) Human anti-self antibodies with high specificity from phage display libraries. EMBO J. 12, 725-734.
    • (1993) EMBO J. , vol.12 , pp. 725-734
    • Griffiths, A.D.1    Malmqvist, M.2    Marks, J.D.3
  • 14
    • 0027365756 scopus 로고
    • Determination of the relative binding affinity of influenza virus N9 sialidases with the Fab fragment of monoclonal antibody NC41 using biosensor technology
    • Gruen, L.C., Kortt, A.A. and Nice, E. (1994) Determination of the relative binding affinity of influenza virus N9 sialidases with the Fab fragment of monoclonal antibody NC41 using biosensor technology. Eur. J. Biochem. 217, 319-325.
    • (1994) Eur. J. Biochem. , vol.217 , pp. 319-325
    • Gruen, L.C.1    Kortt, A.A.2    Nice, E.3
  • 15
    • 0015315530 scopus 로고
    • Antibody affinity. III The role of multivalence
    • Hornick, C.L. and Karush, F. (1972) Antibody affinity. III The role of multivalence. Immunochem. 9, 325-340.
    • (1972) Immunochem. , vol.9 , pp. 325-340
    • Hornick, C.L.1    Karush, F.2
  • 16
    • 0029155283 scopus 로고
    • A single amino acid substitution at N-terminal region of coat-protein of turnip mosaic virus alters antigenicity and aphid transmissibility
    • Kantrong, S.S-H., Briand, J.P. and Sako, N. (1995) A single amino acid substitution at N-terminal region of coat-protein of turnip mosaic virus alters antigenicity and aphid transmissibility. Arch. Virol. 140, 453-467.
    • (1995) Arch. Virol. , vol.140 , pp. 453-467
    • Kantrong, S.S.-H.1    Briand, J.P.2    Sako, N.3
  • 17
    • 0016139612 scopus 로고
    • Fowl plague virus replication in mammalian cell-erythocyte heterokaryons: Studies concerning the actinomycin D and ultra-violet sensitive phase in influenza virus replication
    • Kelly, D.C. and Dimmock, N.J. (1974) Fowl plague virus replication in mammalian cell-erythocyte 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
  • 18
    • 0002696842 scopus 로고
    • Boardman, D. (Ed.) A. Wiley and Sons, Chichester
    • Kovacs, G. (1982) In Boardman, D. (Ed.) Electromagnetic Surface Modes, A. Wiley and Sons, Chichester, p. 143.
    • (1982) Electromagnetic Surface Modes , pp. 143
    • Kovacs, G.1
  • 19
    • 0028957940 scopus 로고
    • Protection from lethal coronavirus infection by immunoglobulin fragments
    • Lamarre, A. and Talbot, P.J. (1995) Protection from lethal coronavirus infection by immunoglobulin fragments. J. Immunol. 154, 3975-3984.
    • (1995) J. Immunol. , vol.154 , pp. 3975-3984
    • Lamarre, A.1    Talbot, P.J.2
  • 20
    • 0027772267 scopus 로고
    • Biological activity, binding site and affinity of monoclonal antibodies to the fusion protein of respiratory syncytial virus
    • Lounsbach, G.R., Bourgeois, C., West, W.H.L. et al. (1994) Biological activity, binding site and affinity of monoclonal antibodies to the fusion protein of respiratory syncytial virus. J. Gen. Virol. 74, 2559-2565.
    • (1994) J. Gen. Virol. , vol.74 , pp. 2559-2565
    • Lounsbach, G.R.1    Bourgeois, C.2    West, W.H.L.3
  • 21
    • 0027237482 scopus 로고
    • Measurement of cerebrospinal fluid antibody to the HIV-1 principle neutralizing determinant V3 loop
    • Lucey, D.R., VanCott, T.C., Loomis, L.D. et al. (1993) Measurement of cerebrospinal fluid antibody to the HIV-1 principle neutralizing determinant V3 loop. J. AIDS 6.
    • (1993) J. AIDS , vol.6
    • Lucey, D.R.1    VanCott, T.C.2    Loomis, L.D.3
  • 23
    • 0028360038 scopus 로고
    • Effect of HIV-1 peptide presentation on the affinity constants of two monoclonal antibodies determined by BIAcore technology
    • Mani, J.-C., Marchi, V. and Cucurou, C. (1994) Effect of HIV-1 peptide presentation on the affinity constants of two monoclonal antibodies determined by BIAcore technology. Mol. Immunol. 31, 439-444.
    • (1994) Mol. Immunol. , vol.31 , pp. 439-444
    • Mani, J.-C.1    Marchi, V.2    Cucurou, C.3
  • 24
    • 0028917784 scopus 로고
    • Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120
    • Moore, J.P., Cao, Y., Quing, L. et al. (1995) Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120. J. Virol. 69, 101-109.
    • (1995) J. Virol. , vol.69 , pp. 101-109
    • Moore, J.P.1    Cao, Y.2    Quing, L.3
  • 25
    • 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. and 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
  • 27
    • 0021042615 scopus 로고
    • On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b fron BALB/c mice
    • Parham, P. (1983) On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b fron BALB/c mice. J. Immunol. 131, 2895-2902.
    • (1983) J. Immunol. , vol.131 , pp. 2895-2902
    • Parham, P.1
  • 28
    • 0027422957 scopus 로고
    • Measurement of kinetic binding constants of viral antibodies using new biosensor technology
    • Pellequer, J.L. and Van Regenmortel, M.H.V. (1993) Measurement of kinetic binding constants of viral antibodies using new biosensor technology. J. Immunol. Methods 166, 133-143.
    • (1993) J. Immunol. Methods , vol.166 , pp. 133-143
    • Pellequer, J.L.1    Van Regenmortel, M.H.V.2
  • 29
    • 0028122633 scopus 로고
    • Development of cowpea mosaic virus as a high yielding system for the presentation of foreign peptides
    • Porta, C., Spall, V.E., Loveland, J. et al. (1994) Development of cowpea mosaic virus as a high yielding system for the presentation of foreign peptides. Virology 202, 949-955.
    • (1994) Virology , vol.202 , pp. 949-955
    • Porta, C.1    Spall, V.E.2    Loveland, J.3
  • 30
    • 0027424056 scopus 로고
    • Verification of the intraction between peptide T and CD4 using surface plasmon resonance
    • Ramsdale, T.E., Andrews, P.R. and Nice, E.C. (1993) Verification of the intraction between peptide T and CD4 using surface plasmon resonance. FEBS Letts. 333, 217-222.
    • (1993) FEBS Letts. , vol.333 , pp. 217-222
    • Ramsdale, T.E.1    Andrews, P.R.2    Nice, E.C.3
  • 31
    • 0028135460 scopus 로고
    • Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA
    • Richalet, S.E., Cordel, P.M., Zeder-Lutz, G. et al. (1994) Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA. J. Immunol. Methods 176, 221-234.
    • (1994) J. Immunol. Methods , vol.176 , pp. 221-234
    • Richalet, S.E.1    Cordel, P.M.2    Zeder-Lutz, G.3
  • 32
    • 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 III, C.F. and 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. J. Virol. 68, 4821-4828.
    • (1994) J. Virol. , vol.68 , pp. 4821-4828
    • Roben, P.1    Moore, J.P.2    Sodroski, J.3    Barbas C.F. III4    Burton, D.R.5
  • 33
    • 0028999803 scopus 로고
    • Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer
    • Sattentau, Q.J. and Moore, J.P. (1995) Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J. Exp. Med. 182, 185-196.
    • (1995) J. Exp. Med. , vol.182 , pp. 185-196
    • Sattentau, Q.J.1    Moore, J.P.2
  • 34
    • 85030274527 scopus 로고    scopus 로고
    • Influenza A virus epitopes vary in neutralization efficiency
    • in press
    • Schofield, D.J. and Dimmock, N.J. (1996) Influenza A virus epitopes vary in neutralization efficiency. Proc. Natl. Acad. Sci., in press.
    • (1996) Proc. Natl. Acad. Sci.
    • Schofield, D.J.1    Dimmock, N.J.2
  • 35
    • 0025187054 scopus 로고
    • Specific structural alteration of the influenza haemagglutinin by amantadine
    • Sugrue, R.J., Bahadur, G., Zambon, M.C., Hall-Smith, M., Douglas, A.R. and Hay, A.J. (1990) Specific structural alteration of the influenza haemagglutinin by amantadine. EMBO J. 9, 3469-3476.
    • (1990) EMBO J. , vol.9 , pp. 3469-3476
    • Sugrue, R.J.1    Bahadur, G.2    Zambon, M.C.3    Hall-Smith, M.4    Douglas, A.R.5    Hay, A.J.6
  • 36
    • 0028962485 scopus 로고
    • Evidence of a major neutralizable conformational epitope region on VP2 of infectious pancreatic necrosis virus
    • Tarrab, E., Berthiaume, L., Grothe, S., O'Connor-McCourt, M., Heppell, J. and Le Comte, J. (1995) Evidence of a major neutralizable conformational epitope region on VP2 of infectious pancreatic necrosis virus. J. Gen. Virol. 76, 551-558.
    • (1995) J. Gen. Virol. , vol.76 , pp. 551-558
    • Tarrab, E.1    Berthiaume, L.2    Grothe, S.3    O'Connor-McCourt, M.4    Heppell, J.5    Le Comte, J.6
  • 37
    • 0023391217 scopus 로고
    • Quantitative relationships between an influenza virus and neutralizing antibody
    • Taylor, H.P., Armstrong, S.J. and Dimmock, N.J. (1987) Quantitative relationships between an influenza virus and neutralizing antibody. Virology 159, 288-298.
    • (1987) Virology , vol.159 , pp. 288-298
    • Taylor, H.P.1    Armstrong, S.J.2    Dimmock, N.J.3
  • 38
    • 0028133526 scopus 로고
    • Toplogy of bovine rotavirus RF strain VP6 epitopes by real-time biospecific interaction analysis
    • Tosser, G., Delaunay, T., Kohli, E., Grosclaude, J., Pothier, P. and Cohen, J. (1994) Toplogy of bovine rotavirus RF strain VP6 epitopes by real-time biospecific interaction analysis. Virology 204, 8-16.
    • (1994) Virology , vol.204 , pp. 8-16
    • Tosser, G.1    Delaunay, T.2    Kohli, E.3    Grosclaude, J.4    Pothier, P.5    Cohen, J.6
  • 39
    • 0028290323 scopus 로고
    • Dissociation rate of antibody-gp120 binding interactions is predictive of V3-mediated neutralization of HIV-1
    • VanCott, T.C., Bethke, F.R., Polonis, V.R. et al. (1994) Dissociation rate of antibody-gp120 binding interactions is predictive of V3-mediated neutralization of HIV-1. J. Immunol. 153, 449-459.
    • (1994) J. Immunol. , vol.153 , pp. 449-459
    • VanCott, T.C.1    Bethke, F.R.2    Polonis, V.R.3
  • 40
    • 0026512536 scopus 로고
    • Real-time interaction analysis of antibody reactivity to peptides from the envelope glycoprotein, gp160, of HIV-1
    • VanCott, T.C., Loomis, L.D., Redfield, R.R. and Birx, D.L. (1992) Real-time interaction analysis of antibody reactivity to peptides from the envelope glycoprotein, gp160, of HIV-1. J. Immunol. Methods 146, 163-176.
    • (1992) J. Immunol. Methods , vol.146 , pp. 163-176
    • VanCott, T.C.1    Loomis, L.D.2    Redfield, R.R.3    Birx, D.L.4
  • 41
    • 0002154656 scopus 로고
    • Surface plasmon polaritons and their uses
    • Welford, K. (1991) Surface plasmon polaritons and their uses. Opt. Quant. Elect. 23, 1-6.
    • (1991) Opt. Quant. Elect. , vol.23 , pp. 1-6
    • Welford, K.1


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