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 journalArticle

17 Citations (Scopus)

Abstract

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
Volume226
Issue number2
DOIs
Publication statusPublished - 2003 Sep 26

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All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology
  • Genetics

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