Removal of a C-terminal Serine Residue Proximal to the Inter-chain Disulfide Bond of a Human IgG1 Lambda Light Chain Mediates Enhanced Antibody Stability and Antibody Dependent Cell-mediated Cytotoxicity

Shen, Y, et al., Apr 8, 5(3), MAbs, 2013

Sequence and structural analysis of human IgG1 λ constant domains suggest three possible mutations in residues proximal to the lambda Lc cysteine may contribute to disulfide bond stability. Here, deletion of the C-terminal serine of lambda constant region is shown to improve stability of the disulfide bond between the light chain and heavy chain at elevated temperature and pH. This mutation also improves transient expression levels and purification yields of IgG1 λ as well as improved Fc function. Protein A biosensors and the Octet platform were used to determine IgG1 λ levels in culture supernatant.

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