1887

Abstract

The relationship between the efficiency of the neutralization process and the affinity of five monoclonal IgG antibodies specific for the haemagglutinin of type A influenza virus has been investigated by determining their neutralization rate constants (K.) and affinities (K). We addressed the hypothesis that if antibody affinity alone determined the efficiency of neutralization, then the K.:K. ratio would be the same for all antibodies. However, we found that the K.:K. ratio varied by up to 125-fold, suggesting that properties unique to the epitope are of major importance in determining the efficiency of neutralization. These data suggest that vaccines should preferentially stimulate antibodies to epitopes that mediate the most efficient neutralization, and that a high K. should be an important but secondary consideration.

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1997-10-01
2021-10-23
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References

  1. Armstrong S. J., Dimmock N. J. 1992; Neutralization of influenza virus by low concentrations of HA-specific polymeric IgA inhibits viral fusion activity but activation of the ribonucleoprotein is also inhibited. Journal of Virology 66:3823–3832
    [Google Scholar]
  2. Askonas B. A., Taylor P. M., Esquivel F. 1988; Cytotoxic T cells in influenza infection. Annals of the New York Academy of Sciences 532:230–237
    [Google Scholar]
  3. Barbas C. F.III Hu D., Dunlop N., Sawyer L., Cababa D., Hendry R. M., Nara P. L., Burton D. R. 1994; In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain specificity. Proceedings of the National Academy of Sciences USA: 913809–3813
    [Google Scholar]
  4. Brown L. E., Murray J. M., White D. O., Jackson D. C. 1990; An analysis of the properties of monoclonal antibodies directed to epitopes on influenza virus hemagglutinin. Archives of Virology 114:1–26
    [Google Scholar]
  5. Burton D. R., Pyati J., Koduri R., Sharp S. J., Thornton G. B., Parren P. W. H. I., Sawyer L. S. W., Hendry R. M., Dunlop N., Nara P. L., Lamacchia M., Garratty E., Stiehm E. R., Bryson Y., Cao Y., Moore J. P., Ho D. D., Barbas C. F.III 1994; Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 266:1024–1027
    [Google Scholar]
  6. Conley A. J., Gorny M. K., Kessler J. A., Boots L. J., Ossorio-Castro M., Koenig S., Lineberger D. W., Emini E., Williams C., Zolla-Pazner S. 1994; Neutralization of primary human immunodeficiency virus type 1 isolates by the broadly reactive anti-V3 antibody, 447-52D. Journal of Virology 68:6994–7000
    [Google Scholar]
  7. Dimmock N. J. 1993; Neutralization of animal viruses. Current Topics in Microbiology and Immunology 183:1–149
    [Google Scholar]
  8. Dimmock N. J. 1995; Update on the neutralization of animal viruses. Reviews in Medical Virology 5:165–179
    [Google Scholar]
  9. Ditzel H. J., Binley J. M., Moore J. P., Sodroski J., Sullivan N., Sawyer L. S. W., Hendry R. M., Yang W.-P., Barbas C. F.III Burton D. R. 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. Journal ofImmunology 154:895–908
    [Google Scholar]
  10. Dulbecco R., Vogt M., Strickland A. G. R. 1956; A study of the basic aspects of neutralization of two animal viruses, Western equine encephalitis virus and poliomyelitis virus. Virology 2:162–205
    [Google Scholar]
  11. Ey P. L., Prowse S. J., Jenkin C. R. 1978; Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-Sepharose. Immunochemistry 15:429–436
    [Google Scholar]
  12. Fazekas de St Groth S., Webster R. G. 1963; The neutralization of animal viruses. IV. Parameters of the influenza virus-antibody system. Journal of Immunology 90:151–164
    [Google Scholar]
  13. Frankel M. E., Gerhard W. 1979; The rapid determination of binding constants for antiviral antibodies by a radioimmunoassay. An analysis of the interaction between hybridoma proteins and influenza virus. Molecular Immunology 16:101–106
    [Google Scholar]
  14. Friguet B., Chaffotte A. F., Djavadi-Ohaniance L., Goldberg M. E. 1985; Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. Journal of Immunological Methods 77:305–319
    [Google Scholar]
  15. Icenogle J. C., Shiwen H., Duke G., Gilbert S., Rueckert R., Anderegg J. 1983; Neutralization of poliovirus by a monoclonal antibody: kinetics and stoichiometry. Virology 127:412–425
    [Google Scholar]
  16. Kelly D. C., 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
    [Google Scholar]
  17. Kilbourne E. D. 1987 Influenza New York: Plenum Medical Book Co;
    [Google Scholar]
  18. McInerney T. L., McLain L. Armstrong, 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
    [Google Scholar]
  19. McLain L., Dimmock N. J. 1994; Single- and multi-hit kinetics of immunoglobulin G neutralization of human immunodeficiency virus type 1 by monoclonal antibodies. Journal of General Virology 75:1457–1460
    [Google Scholar]
  20. Moore J. P., Sattentau Q. J., Wyatt R., Sodroski J. 1994; Mapping the topology of the human immunodeficiency virus glycoprotein gp120 with a panel of monoclonal antibodies. Journal of Virology 68:469–484
    [Google Scholar]
  21. Moore J. P., Cao Y., Quing L., Sattentau Q. J., Pyati J., Koduri R., Robinson J., Barbas C. F.III Burton D. R., Ho D. D. 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. Journal of Virology 69:101–109
    [Google Scholar]
  22. Nakamura G. R., Byrn R., Wilkes D. M., Fox J. A., Hobbs H. R., Hastings M. C., Norcross M. A., Fendly B. M., Berman P. W. 1993; Strain specificity and binding affinity requirements of neutralizing antibodies to the C4 domain of gp120 from human immunodeficiency virus type 1. Journal of Virology 67:6179–6191
    [Google Scholar]
  23. Outlaw M. C., Dimmock N. J. 1991; Insights into neutralization of animal viruses gained from the study of influenza viruses. Epidemiology and Infection 106:205–220
    [Google Scholar]
  24. Outlaw M. C., Dimmock N. J. 1993; IgG -neutralization of type A influenza viruses and the inhibition of the endosomal fusion stage of the infectious pathway. Virology 195:413–421
    [Google Scholar]
  25. 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
    [Google Scholar]
  26. Parren P. W. H. I., Ditzel H. J., Gulizia R. J., Barbas C. F.III Burton D. R., Mosier D. E. 1995; Protection against HIV-1 infection in hu- PBL-SCID mice by passive immunization with a neutralizing monoclonal antibody against the gp120 CD4 binding site. AIDS 9:F1–6
    [Google Scholar]
  27. Potter C. W. 1994; Attenuated influenza virus vaccines. Reviews in Medical Virology 4:279–292
    [Google Scholar]
  28. Rigg R. J., Carver A. S., Dimmock N. J. 1989; IgG-neutralized influenza virus undergoes primary, but not secondary uncoating in vivo. Journal of General Virology 70:2097–2109
    [Google Scholar]
  29. 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
    [Google Scholar]
  30. Sattentau Q. J., Moore J. P. 1995; Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. Journal of Experimental Medicine 182:185–196
    [Google Scholar]
  31. 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
    [Google Scholar]
  32. Stamatatos L., Cheng-Mayer C. 1995; (1) Structural modifications of the envelope of gp120 glycoprotein of human immunodeficiency virus type 1 upon oligomerization and (2) differential V3 loop epitope exposure of isolates displaying distinct tropism upon virion-soluble receptor binding. Journal of Virology 69:6191–6198
    [Google Scholar]
  33. Stevens F. J. 1987; Modification of an ELISA-based procedure for affinity determination: correction necessary for use with bivalent antibody. Molecular Immunology 24:1055–1060
    [Google Scholar]
  34. Sugrue R. J., Bahadur G., Zambon M. C., Hall-Smith M., Douglas A. R., Hay A. J. 1990; Specific structural alteration of the influenza haemagglutinin by amantadine. EMBO Journal 9:3469–3476
    [Google Scholar]
  35. Taylor H. P., Armstrong S. J., Dimmock N. J. 1987; Quantitative relationships between an influenza virus and neutralizing antibody. Virology 159:288–298
    [Google Scholar]
  36. Ueki Y., Goldfarb I. S., Harindranath N., Gore M., Koprowski H., Notkins A. L., Casali P. 1990; Clonal analysis of a human antibody response: quantitation of precursors of antibody-producing cells and generation and characterization of monoclonal IgM, IgG and IgA to rabies virus. Journal of Experimental Medicine 171:19–34
    [Google Scholar]
  37. VanCott T. C., Bethke F. R., Polonis V. R., Gorny M. K., Zolla-Pazner S., Redfield R. R., Birx D. L. 1994; Dissociation rate of antibody-gp120 binding interactions is predictive of V3-mediated neutralization of HIV-1. Journal of Immunology 153:449–459
    [Google Scholar]
  38. Webster R. G., Bean W. J., Gorman O. T., Chambers T. M., Kawaoka Y. 1992; Evolution and ecology of influenza A viruses. Microbiological Reviews 56:152–179
    [Google Scholar]
  39. Wells M. A., Albrecht P., Ennis F. A. 1981; Recovery from a viral respiratory tract infection. I Influenza pneumonia in normal and T cell- deficient mice. Journal of Immunology 126:1036–1041
    [Google Scholar]
  40. 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
    [Google Scholar]
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