Bacterial cell surface display for epitope mapping of hepatitis C virus core antigen

Su Min Kang, Jin Kyu Rhee, Eui Joong Kim, Kwang Hyub Han, Jong Won Oh

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Cell surface expression of protein has been widely used to display enzymes and antigens. Here we show that Pseudomonas syringae ice nucleation protein with a deletion of internal repeating domain (INC) can be used in Escherichia coli to display peptide in a conformationally active form on the outside of the folded protein by fusing to the C-terminus of INC. Diagnostic potential of this technology was demonstrated by effective mapping of antigenic epitopes derived from hepatitis C virus (HCV) core protein. Amino acids 1-38 and 26-53 of HCV core protein were found to react more sensitively in a native conformation with the HCV patient sera than commercial diagnostic antigen, c22p (amino acids 10-53) by display-ELISA. These results demonstrate that the bacterial cell surface display using INC is useful for peptide presentation and thus epitope mapping of antigen.

Original languageEnglish
Pages (from-to)347-353
Number of pages7
JournalFEMS Microbiology Letters
Issue number2
StatePublished - 26 Sep 2003

Bibliographical note

Funding Information:
This work was supported in part by Genofocus Inc., Daejeon, Korea, as a part of the National Research Lab project (M1-0104-00-0144) granted from Korea Ministry of Science and Technology.


  • Bacteria cell surface display
  • Diagnosis
  • Epitope mapping
  • HCV core protein
  • Ice nucleation protein
  • Peptide display


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