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 language | English |
|---|---|
| Pages (from-to) | 347-353 |
| Number of pages | 7 |
| Journal | FEMS Microbiology Letters |
| Volume | 226 |
| Issue number | 2 |
| DOIs | |
| State | Published - 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.
Keywords
- Bacteria cell surface display
- Diagnosis
- Epitope mapping
- HCV core protein
- Ice nucleation protein
- Peptide display