Affinity maturation of an anti-hepatitis B virus PreS1 humanized antibody by phage display

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Title
Affinity maturation of an anti-hepatitis B virus PreS1 humanized antibody by phage display
Author(s)
G H Yang; S O Yoon; M H Jang; Hyo Jeong Hong
Bibliographic Citation
Journal of Microbiology, vol. 45, no. 6, pp. 528-533
Publication Year
2007
Abstract
In a previous study we generated an anti-Hepatitis B Virus (HBV) preS1 humanized antibody (HzKR127) that showed in vivo HBV-neutralizing activity in chimpanzees. However, the antigen-binding affinity of the humanized antibody may not be sufficient for clinical use and thus affinity maturation is required for better therapeutic efficacy. In this study, phage display technique was employed to increase the affinity of HzKR127. All six amino acid residues (Glu95-Tyr96-Asp97-Glu98-Ala99-Tyr100) in the heavy (H) chain complementarydetermining region 3 (HCDR3) of HzKR127 were randomized and phage-displayed single chain Fv (scFv) library was constructed. After three rounds of panning, 12 different clones exhibiting higher antigen-binding activity than the wild type ScFv were selected and their antigen-binding specificity for the preS1 confirmed. Subsequently, five ScFv clones were converted to whole IgG and subjected to affinity determination. The results showed that two clones (B3 and A19) exhibited an approximately 6 fold higher affinities than that of HzKR127. The affinity-matured humanized antibodies may be useful in anti-HBV immunotherapy.
ISSN
1225-8873
Publisher
Microbiological Society Korea
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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