Journal
JOURNAL OF IMMUNOLOGICAL METHODS
Volume 329, Issue 1-2, Pages 176-183Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jim.2007.10.009
Keywords
monoclonal antibody; phage display; epitope tag; hepatitis B virus preS1; affinity maturation
Categories
Ask authors/readers for more resources
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 preS I epitope. Mice were immunized with the N-terminal domain of human thrombopoietin fused to the S I 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 (K-D 1.2 nM) for preS1 compared with KR127 (K-D 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. (C) 2007 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available