Some Aspects of Antibody-Antigen Reactions and Theoretical Considerations of the Immunologic Response

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Abstract
The theory of the altered configuration of antibody and antigen upon interaction and the consequent antigenicity of the antibody is reviewed. The use of enzymes as antigens has given suggestive evidence of this change in configuration. More direct evidence indicated that the change in antibody configuration results principally from exposure of thiol groups on the antibody, increased levorotation and an increase in the apparent volume of the antibody similar to that obtained in protein denaturation. The antigenicity of the antibody has been shown for isologous antibody and autologous antibody both with simple protein antigens and with complex cellular antigens. Although the above mentioned theory is supported by the evidence, certain questions are not answered by it. One question concerns the observation that an antigen carrying a particular hapten is capable of stimulating the formation of antibodies that are indifferent to it, but react with the haptenic site on a heterologous protein carrier. It has also been shown that enzymatic activity can be destroyed by an antibody. An antibody to some determinant on a viable cell often destroys the cell, but sometimes it has the opposite effect. There is also a question concerning the association of a blood group determinant in a specific way with an isohemagglutinin directed against another determinant in a specific manner. To answer these questions, the author proposes that the relationship between the corresponding sites on the antibody and antigen, contrary to current concept, are less than complementary, i.e. subcomplementary. The reactive groups on the antibody site do not have the proper orientation and geometry to allow for a perfect fit on the corresponding site on the antigen.

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