Cell surface display of hepatitis B virus surface antigen by using Pseudomonas syringae ice nucleation protein.
A new system designed for cell surface display of recombinant proteins on Escherichia coli was evaluated for expression of eukaryotic viral antigens. The major surface antigen of hepatitis B virus (HBsAg) was fused to the ice nucleation protein (INP), an outer membrane protein of Pseudomonas syringae. Western blotting, immunofluorescence microscopy, whole-cell ELISA, and ice nucleation activity assay confirmed expression of recombinant proteins on the surface of Escherichia coli. This study indicated that INP-based cell surface display can be used for epitope mapping and recombinant bacteria expressing hepatitis viral antigens may be used for developing live vaccines.
Kim
E J
EJ
Department of Biotechnology, College of Engineering and Bioproducts Research Center, Yonsei University, Seoul, Korea.
Yoo
S K
SK
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000378:metabolism*; D015153:Blotting, Western; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D006514:Hepatitis B Surface Antigens / Q000235:genetics* / Q000276:immunology / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D010957:Plasmids; D011549:Pseudomonas / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000276:immunology / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D006514:Hepatitis B Surface Antigens; D011993:Recombinant Fusion Proteins; C063113:ice nucleation protein