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Antigenic determinants resulting from polymerization of immunoglobulin G
1Central Laboratory for Clinical Investigation, Osaka University Medical School, Japan.
Japanese Journal of Medical Science & Biology
|October 1, 1988
Summary
Researchers developed antibodies against aggregated human IgG (AHG) and immune complexes (IC). A common determinant was found shared between AHG and tetanus toxoid-antitoxin (T/aT) immune complexes, indicating shared antigenic structures.
Area of Science:
- Immunology
- Biochemistry
Background:
- Antibodies play a crucial role in the immune response.
- Immune complexes (IC) and aggregated immunoglobulins can elicit specific antibody responses.
Purpose of the Study:
- To investigate the antigenic properties of aggregated human IgG (AHG) and immune complexes (IC).
- To identify potential shared determinants between different forms of human IgG and ICs.
Main Methods:
- Antibodies were raised against heat-aggregated human IgG (AHG) and tetanus toxoid-antitoxin (T/aT) immune complexes (IC) in rabbits and mice.
- Ouchterlony double diffusion technique was employed to analyze antisera against native monomeric human IgG (NHG), AHG, and chemically linked IgG (poly-G).
Main Results:
- The study demonstrated the appearance of neoantigens on human IgG when bound to its antigen or denatured.
- Results indicated a common antigenic determinant shared between AHG and T/aT ICs, in addition to their unique determinants.
Conclusions:
- Human IgG exhibits neoantigens upon aggregation or complex formation.
- A shared determinant exists between aggregated IgG and specific immune complexes, suggesting common structural features.
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