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Structural analysis of the epitopes recognized by monoclonal antibodies to angiotensin II.

P O Couraud
J Immunol May 1, 1986, 136 (9) 3365-3370;
P O Couraud
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Abstract

Six clones were obtained that secrete anti-angiotensin II antibodies after somatic cell fusions between splenocytes of immunized BALB/c or outbred OF1 mice and NS-1 myeloma cells. The dissociation constants for angiotensin II ranged from 0.3 to 2.9 nM. A panel of 20 structural analogs of the hormone were used as probes to analyze the specificity of binding. From the binding studies and the putative three-dimensional structures of the tested peptides, three families of antibodies could be distinguished that recognized overlapping epitopes; the conservation of the native conformation of the angiotensin II molecule in the analogs appeared essential for the preservation of a high affinity to the antibodies. With one antibody, the affinities of the angiotensin II analogs have been correlated with their intrinsic biologic activities (as measured by in vivo pressor tests), and not with their binding affinity to the membrane receptor. These results are interpreted as mimicry, by the antibody binding site, of the active conformation of the receptor site.

  • 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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Structural analysis of the epitopes recognized by monoclonal antibodies to angiotensin II.
P O Couraud
The Journal of Immunology May 1, 1986, 136 (9) 3365-3370;

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Structural analysis of the epitopes recognized by monoclonal antibodies to angiotensin II.
P O Couraud
The Journal of Immunology May 1, 1986, 136 (9) 3365-3370;
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Print ISSN 0022-1767        Online ISSN 1550-6606