Efficient cell surface display of organophosphorous hydrolase using N-terminal domain of ice nucleation protein in Escherichia coli

2008 ◽  
Vol 25 (4) ◽  
pp. 804-807 ◽  
Author(s):  
Dong Gyun Kang ◽  
Lin Li ◽  
Jeong Hyub Ha ◽  
Suk Soon Choi ◽  
Hyung Joon Cha
2011 ◽  
Vol 108 (12) ◽  
pp. 2853-2864 ◽  
Author(s):  
Li-Hai Fan ◽  
Ning Liu ◽  
Ming-Rui Yu ◽  
Shang-Tian Yang ◽  
Huan-Lin Chen

1999 ◽  
Vol 6 (4) ◽  
pp. 499-503 ◽  
Author(s):  
Young-Don Kwak ◽  
Seung-Ku Yoo ◽  
Eui-Joong Kim

ABSTRACT A new system designed for cell surface display of recombinant proteins on Escherichia coli has been evaluated for expression of eukaryotic viral proteins. Human immunodeficiency virus type 1 (HIV-1) gp120 was fused to the C terminus of ice nucleation protein (INP), an outer membrane protein of Pseudomonas syringae. Western blotting, immunofluorescence microscopy, fluorescence-activated cell-sorting analysis, whole-cell enzyme-linked immunosorbent assay, and ice nucleation activity assay confirmed the successful expression of HIV-1 gp120 on the surface ofEscherichia coli. This study shows that the INP system can be used for the expression of eukaryotic viral proteins. There is also a possibility that the INP system can be used as an AIDS diagnostic system, an oral vaccine delivery system, and an expression system for various heterologous higher-molecular-weight proteins.


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