A new algorithm to convert a normal antibody into the corresponding catalytic antibody release_2wjuhkbqbfc4rmo7kgmmgazmsm

by Emi Hifumi, Hiroaki Taguchi, Haruna Tsuda, Tetsuro Minagawa, Tamami Nonaka, Taizo Uda

Published in Science Advances by American Association for the Advancement of Science (AAAS).

2020   Volume 6, Issue 13, eaay6441


Over thousands of monoclonal antibodies (mAbs) have been produced so far, and it would be valuable if these mAbs could be directly converted into catalytic antibodies. We have designed a system to realize the above concept by deleting Pro<jats:sup>95</jats:sup>, a highly conserved residue in CDR-3 of the antibody light chain. The deletion of Pro<jats:sup>95</jats:sup> is a key contributor to catalytic function of the light chain. The S35 and S38 light chains have identical amino acid sequences except for Pro<jats:sup>95</jats:sup>. The former, with Pro<jats:sup>95</jats:sup> did not show any catalytic activity, whereas the latter, without Pro<jats:sup>95</jats:sup>, exhibited peptidase activity. To verify the generality of this finding, we tested another light chain, T99wt, which had Pro<jats:sup>95</jats:sup> and showed little catalytic activity. In contrast, a Pro<jats:sup>95</jats:sup>-deleted mutant enzymatically degraded the peptide substrate and amyloid-beta molecule. These two cases demonstrate the potential for a new method of creating catalytic antibodies from the corresponding mAbs.
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Date   2020-03-25
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