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Title 

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

Authors 

Seung-Wook ChiJ KimG S YiHyo Jeong HongS E Ryu

Publisher 

Elsevier

Issue Date 

2009

Citation 

FEBS Letters, vol. 583, no. 18, pp. 3095-3100

Keywords 

EpitopeHepatitis B virusNeutralizing antibodyNuclear magnetic resonancepreS1

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.

ISSN 

0014-5793

Link 

http://dx.doi.org/10.1016/j.febslet.2009.08.030

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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