Broadly neutralizing anti-HBV antibody binds to non-epitope regions of preS1

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Title
Broadly neutralizing anti-HBV antibody binds to non-epitope regions of preS1
Author(s)
Seung-Wook Chi; J Kim; G S Yi; Hyo Jeong Hong; S E Ryu
Bibliographic Citation
FEBS Letters, vol. 583, no. 18, pp. 3095-3100
Publication Year
2009
Abstract
Broadly neutralizing anti-hepatitis B virus (HBV) antibody HzKR127 undergoes a fairly large conformational change of CDR H3 loop upon binding to HBV preS1 epitope peptide. In this study, we identified low-affinity antibody-binding sites in the largely unstructured preS1 region by nuclear magnetic resonance and biochemical studies, indicating that the antibody binds to the preS1 region outside the major immune epitope with low affinity. Surface plasma resonance experiments showed that the full-length preS1 has approximately three fold higher affinity for HzKR127 Fab than the preS1 epitope peptide, suggesting that the presence of low-affinity sites in the preS1 region increases the antibody-binding affinity. Therefore, the low-affinity binding of the antibody to non-epitope regions of preS1 may contribute to effective neutralization.
Keyword
EpitopeHepatitis B virusNeutralizing antibodyNuclear magnetic resonancepreS1
ISSN
0014-5793
Publisher
Wiley
DOI
http://dx.doi.org/10.1016/j.febslet.2009.08.030
Type
Article
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
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