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Studies on the Immunogenicity of Antigen-Antibody Precipitates

1. The Suppressive Effect of anti-L and anti-H Chain Antibodies on the Immunogenicity of Human G Globulin¹

From the Children's Asthma Research Institute and Hospital, Denver, Colorado

Abstract

Guinea pigs immunized with antibody excess immune precipitates of human G globulin (HGG) and rabbit or guinea pig anti-F_ab or anti-F_c antibody make little antibody to HGG. The small amount of anti-HGG antibody produced in each case was directed against antigenic determinants present in both the F_ab and F_c portions of the HGG molecule, and thus bore no reflection on the specificity of the antibody in the complexes. This finding suggests that the suppression is to the whole antigen molecule rather than its individual antigenic determinants.

The mechanism of the suppression of antibody formation to complexes comprised of immunogenic components cannot be explained in terms of antigenic competition for antibody-producing cells, nor in terms of "blocking" of antigenic determinants. It was shown that the combination of HGG with specific anti-F_ab antibody at the equivalence point hinders only 21% of the F_c antigenic determinant, while in 4-fold antibody excess precipitates 66% of the F_c antigenic determinants are still capable of reacting with homologous antibody. Similarly, equivalence precipitates of HGG with anti-F_c antibody "block" only 16% of F_ab determinants, whereas in 4-fold antibody excess precipitates 43% of the F_ab determinants are "hidden."

Quantitatively, HGG bound in a 4-fold antibody excess precipitate with either anti-F_ab or anti-F_c antibody has approximately 0.5% of the immunogenicity of the uncombined antigen. It thus appears that antigen in antibody excess immune precipitates is non-immunogenic, and that the antibody produced against HGG can be explained in terms of a 0.5% dissociation of the complex in vivo.

Footnotes

This work was supported by Grant AI-04985 from the United States Public Health Service.