Enhanced humanization and affinity maturation of neutralizing anti-hepatitis B virus preS1 antibody based on antigen-antibody complex structure
- Authors
- Kim, Jin Hong; Gripon, Philippe; Bouezzedine, Fidaa; Jeong, Mun Sik; Chi, Seung-Wook; Ryu, Seong-Eon; Hong, Hyo Jeong
- Issue Date
- Jan-2015
- Publisher
- WILEY
- Keywords
- Humanized antibody; Specificity-determining residue grafting; Affinity maturation; Hepatitis B virus; preS1; Virus neutralization
- Citation
- FEBS LETTERS, v.589, no.2, pp.193 - 200
- Indexed
- SCIE
SCOPUS
- Journal Title
- FEBS LETTERS
- Volume
- 589
- Number
- 2
- Start Page
- 193
- End Page
- 200
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/158178
- DOI
- 10.1016/j.febslet.2014.11.046
- ISSN
- 0014-5793
- Abstract
- 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.
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