Enzymatization of mouse monoclonal antibody to the corresponding catalytic antibody

Catalytic antibodies exhibit unique features for recognizing and degrading antigens. However, the production of these antibodies is time-consuming and labor-intensive. Herein, mouse monoclonal antibodies (mAbs) were converted into catalytic antibodies by deleting Pro95 in the light chain using three antibodies targeting the influenza A virus. Although no catalytic activity was observed for the mAbs and light chains, Pro95-deleted light chains exhibited catalytic activity for cleaving the antigenic peptide. The affinity of the Pro95-deleted light chains for the antigen increased approximately 100-fold compared to that of the wild-type light chains. Notably, the Pro95-deleted mutants suppressed influenza virus infection in the in vitro assay. Molecular modeling suggested that three residues (Asp1, Ser92, and His93) in the mutant moved closer to the appropriate position, enhancing catalytic function and immunoreactivity. Note that a rapid and simple method for generating catalytic antibodies for various diagnostic and therapeutic applications from exiting antibodies were attained.