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Epitope and functional specificity of monoclonal antibodies to mouse interferon-gamma: the synthetic peptide approach.

J K Russell, M P Hayes, J M Carter, B A Torres, B M Dunn, S W Russell and H M Johnson
J Immunol May 1, 1986, 136 (9) 3324-3328;
J K Russell
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M P Hayes
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J M Carter
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B A Torres
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B M Dunn
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S W Russell
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H M Johnson
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Abstract

Spleen cells from hamsters immunized with recombinant mouse interferon-gamma (IFN-gamma) were fused with mouse myeloma cells, resulting in the production of four anti-IFN-gamma monoclonal antibodies. Binding of 125I-IFN-gamma by these protein A-bound antibodies was specifically blocked by cold IFN-gamma. Binding by three of these antibodies was also blocked by a synthetic peptide corresponding to the N-terminal 1-39 amino acids of IFN-gamma, whereas a corresponding C-terminal (95-133) peptide had no effect on binding. The N-terminal specificity of these three antibodies was confirmed by their specific binding of 125I-N-terminal (1-39) peptide. One of the N-terminal specific monoclonal antibodies inhibited both antiviral and macrophage priming (for tumor cell killing) activities of IFN-gamma, whereas the other two had no effect on either biologic function. The selectivity of the inhibition of IFN-gamma function was not due to a differential ability of the N-terminal specific antibodies to bind IFN-gamma. Blocking experiments with cold IFN-gamma and N-terminal peptide suggest that the epitope specificities of the monoclonal antibodies could be determined by the conformational or topographic structure of IFN-gamma. An exact determination of the epitope specificity of the monoclonal antibody that inhibited IFN-gamma function could provide insight into the structural basis for the role of the N-terminal domain in the biologic function of IFN-gamma. Polyclonal antibodies to either the N-terminal or the C-terminal peptides also inhibited both the antiviral and the macrophage-priming activities of IFN-gamma. All of the antibodies that inhibited IFN-gamma function also blocked binding of IFN-gamma to membrane receptor on cells, whereas antibodies that did not block function also did not inhibit binding. The data suggest that both the N-terminal and the C-terminal domains of IFN-gamma play an important role in its antiviral and macrophage-priming functions, possibly in a cooperative manner.

  • Copyright © 1986 by American Association of Immunologists

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The Journal of Immunology
Vol. 136, Issue 9
1 May 1986
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Epitope and functional specificity of monoclonal antibodies to mouse interferon-gamma: the synthetic peptide approach.
J K Russell, M P Hayes, J M Carter, B A Torres, B M Dunn, S W Russell, H M Johnson
The Journal of Immunology May 1, 1986, 136 (9) 3324-3328;

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Epitope and functional specificity of monoclonal antibodies to mouse interferon-gamma: the synthetic peptide approach.
J K Russell, M P Hayes, J M Carter, B A Torres, B M Dunn, S W Russell, H M Johnson
The Journal of Immunology May 1, 1986, 136 (9) 3324-3328;
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Print ISSN 0022-1767        Online ISSN 1550-6606