Affinity Maturation of an Anti-Hepatitis B Virus PreS1 Humanized Antibody by Phage Display

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 req...

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Veröffentlicht in:The journal of microbiology 2007-12, Vol.45 (6), p.528-533
Hauptverfasser: Yang, G.H. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), Yoon, S.O. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), Jang, M.H. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), Hong, H.J. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), E-mail: hjhong@kribb.re.kr
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Sprache:eng
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Zusammenfassung: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 complementary-determining region 3 (HCDR3) of HzKR127 were randomized and phage-displayed single chain Fv (scFv) library was constructed.
ISSN:1225-8873
1976-3794