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Title 

Selection of an affinity-matured antibody against a defined epitope by phage display of an immune antibody library

Authors 

Sang Jick KimM H JangHyun Joo AhnJin-Hong KimJ H LimC J RyuN K LimK S KimM J ParkInsoo ParkHyo Jeong Hong

Publisher 

Elsevier

Issue Date 

2008

Citation 

Journal of Immunological Methods, vol. 329, no. 1, pp. 176-183

Keywords 

affinity maturationepitope taghepatitis B virus preS1monoclonal antibodyphage displayamino acidepitopeimmunoglobulin F(ab) fragmentneutralizing antibodyamino terminal sequence

Abstract 

In a previous study, we generated a murine hepatitis B virus (HBV)-neutralizing monoclonal antibody (mAb), KR127, that binds to an epitope (amino acids 37-45, NSNNPDWDF) of the preS1 antigen. Furthermore, an epitope tag, S1 (NANNPDWDF), was developed for protein tagging. The aim of the present study was to develop a high-affinity antibody to the same preS1 epitope. Mice were immunized with the N-terminal domain of human thrombopoietin fused to the S1 tag (nTPO-S1), and a phage-displayed chimeric Fab library was constructed and screened by panning against nTPO-S1. A high-affinity antibody (3-34) was selected that binds to the preS1 antigen. The IgG molecules of 3-34 showed approximately nine-fold higher affinity (KD 1.2 nM) for preS1 compared with KR127 (KD 10.4 nM), competed with KR127 for binding to the epitope, and bound to HBV particles. This study provides a simple and efficient way to develop a high-affinity antibody to a defined epitope by phage display of an immune antibody library.

ISSN 

0022-1759

Link 

http://dx.doi.org/10.1016/j.jim.2007.10.009

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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