The immune response to a synthetic peptide analogous to the 109–145 βhCG carboxyl-terminus is directed against two major and two minor regions☆

Abstract The immune response to a 37-amino acid synthetic peptide analogous to the carboxyl-terminal part (109–145) of the human chorionic gonadotropin beta subunit (βhCG) was studied with monoclonal antibodies selected from 31 cell fusion experiments. Analysis of the immunogenic determinants borne on the synthetic peptide (CTP) showed a prevailing response to two immunodominant regions. The first was located on the 110–116 amino acid sequence of the CTP which is also the most hydrophilic region: 50% of anti-CTP antibodies selected for their high binding to 125 I βhCG were directed to this sequence. A second immunodominant portion was recognized by four antibodies, and comprised amino acids 134 to 139, representing a highly O -glycosylated region on the native protein. Moreover, a unique antibody designated FB13 bound to a region located on the last seven amino acids (139–145) of βhCG. Finally, a hypothetical conformational determinant was recognized by antibody FB02 within the 121–145 region. Thus, the immune response to CTP was directed against two major and two minor regions. These antigenic determinants were demonstrated to be accessible for antibody binding on both the hCG molecule and its beta subunit. Localization of these epitopes suggests a relationship between the hydrophilicity and the immunological potency of different CTP regions.