Enhanced humanization and affinity maturation of neutralizing anti-hepatitis B virus preS1 antibody based on antigen-antibody complex structure
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- Enhanced humanization and affinity maturation of neutralizing anti-hepatitis B virus preS1 antibody based on antigen-antibody complex structure
- J H Kim; P Gripon; F Bouezzedine; M S Jeong; Seung-Wook Chi; S E Ryu; H J Hong
- Bibliographic Citation
- FEBS Letters, vol. 589, no. 2, pp. 193-200
- Publication Year
- To improve a previously constructed broadly neutralizing hepatitis B virus (HBV)-specific preS1 humanized antibody (HzKR127), we further humanized it through specificity-determining residue (SDR) grafting. Moreover, we improved affinity by mutating two residues in heavy-chain complementarity-determining regions (CDR), on the basis of the crystal structure of the antigen-antibody complex. HzKR127-3.2 exhibited 2.5-fold higher affinity and enhanced virus-neutralizing activity compared to the original KR127 antibody and showed less immunogenic potential than HzKR127. Enhanced virus-neutralizing activity was achieved by the increased association rate, providing insights into engineering potent antibody therapeutics for HBV immunoprophylaxis. HzKR127-3.2 may be a good candidate for HBV immunoprophylaxis.
- Affinity maturationHepatitis B viruspreS1Specificity-determining residue graftingVirus neutralizationHumanized antibody
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- Division of Biomedical Research > 1. Journal Articles
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