Enhanced Humanization and Affinity Maturation of Neutralizing Anti-hepatitis B Virus PreS1 Antibody Based on Antigen-antibody Complex Structure

Kim J, et al., 589(2):193-200, FEBS Lett, 2015

This article describes a biochemical investigation that lead up to an enhancement of the humanized nature and binding affinity of a broadly neutralizing hepatitis B virus (HBV)-specific humanized antibody called HzKR127. Further humanization was achieved by a methodology known as specificity-determining residue (SDR) drafting. The affinity maturation was based on the crystal structure of antigen-antibody complex and that was achieved by mutating two residues in heavy-chain complementarity-determining regions (CDR). An Octet RED system equipped with anti-human Fc-coated biosensor tips was used to capture the antibody. A serial dilution of preS1 fused onto GST was screed against the captured antibody ligand. This study provides insights onto the methods for engineering antibody therapeutics for HBV immunoprophylaxis.

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