Interaction of S17 antibody with the functional binding region of the hepatitis B virus pre-S2 epitope

Chang Yu Chang, Fu Ling Chang, Chen Wei Chiang, Yan Ni Lo, Tsai Yu Lin, Wang Chuan Chen, Keng Chang Tsai, Yu Ching Lee

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


To understand the mechanism for inhibition of hepatitis B virus (HBV) infection is important. In this study, single-chain variable fragment (scFv) antibodies were generated and directed to the pre-S2 epitope of HBV surface antigen (HBsAg). These human scFvs were isolated from a person with history of HBV infection by phage display technology. An evaluation of panning efficiency revealed that the eluted phage titer was increased, indicating that specific clones were enriched after panning. Selected scFvs were characterized with the recombinant HBsAg through Western blotting and enzyme-linked immunosorbent assay to confirm the binding ability. Flow cytometry analysis and immunocytochemical staining revealed that one scFv, S17, could recognize endogenous HBsAg expressed on the HepG2215 cell membrane. Moreover, the binding affinity of scFv S17 to the pre-S2 epitope was determined to be 4.2 10-8 M. Two ion interactions were observed as the major driving forces for scFv S17 interacting with pre-S2 by performing a rational molecular docking analysis. This study provides insights into the structural basis to understand the interactions between an antibody and the pre- S2 epitope. The functional scFv format can potentially be used in future immunotherapeutic applications.

Original languageEnglish
Pages (from-to)492-499
Number of pages8
JournalViral Immunology
Issue number7
Publication statusPublished - Sept 1 2018


  • Hepatitis B virus
  • Molecular docking
  • Phage display technology
  • Pre-S2 epitope
  • Single-chain variable fragment

ASJC Scopus subject areas

  • Immunology
  • Molecular Medicine
  • Virology


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