{'fraction_non_alphanumeric': 0.0283203125, 'fraction_numerical': 0.0537109375, 'mean_word_length': 5.029411764705882, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Antigenic change in a human IgG4‐specific CH3 epitope upon binding of a monoclonal antibody against a neighboring IgG4‐specific epitope

Two sets of monoclonal antibodies (mAbs) probably reacting with two different epitopes in the CH3 domain of the human IgG4 molecule were studied. We observed that the commercially available mAb HP 6011 inhibited the antigen binding of the three mutually inhibitable mAbs, 40‐A2, 41‐E8 and 43‐F11 (40‐series), made by us. However, the 40‐series mAbs, including those with similar affinity such as mAb HP6011, were not able to inhibit mAb HP 6011. When the 40‐series mAbs were preincubated with IgG4, the mAb HP 6011 could partially displace these antibodies. This one‐way inhibition indicates that upon binding mAb HP 6011 changes the antigenic structure of the IgG4 molecule by disrupting the epitope for the 40‐series mAbs. A steric hindrance of this epitope by mAb HP 6011 is more unlikely, since the small Fab fragment of mAb HP 6011 also inhibited the reaction of the 40‐series mAbs.