期刊
FEBS LETTERS
卷 589, 期 2, 页码 193-200出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2014.11.046
关键词
Humanized antibody; Specificity-determining residue grafting; Affinity maturation; Hepatitis B virus; preS1; Virus neutralization
资金
- Ministry of Health and Welfare [A050260]
- Kangwon National University [120140400]
- ANRS (Agence nationale de recherche contre le sida et les hepatites virales)
- Ligue Nationale Contre le Cancer
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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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