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  • Title: Bacterial cell surface display for epitope mapping of hepatitis C virus core antigen.
    Author: Kang SM, Rhee JK, Kim EJ, Han KH, Oh JW.
    Journal: FEMS Microbiol Lett; 2003 Sep 26; 226(2):347-53. PubMed ID: 14553932.
    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.
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