Cell surface display of human immunodeficiency virus type 1 gp120 on Escherichia coli by using ice nucleation protein.
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 of Escherichia 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.
Department of Biotechnology, College of Engineering and Bioproduct Research Center, Yonsei University, 134 Shinchon-Dong, Sudaemun-Ku, Seoul 120-749, Korea.
Y D
YD
Kwak
S K
SK
Yoo
E J
EJ
Kim
D001425:Bacterial Outer Membrane Proteins / Q000494:pharmacology*; D015153:Blotting, Western; D002469:Cell Separation; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods; D004926:Escherichia coli / Q000737:chemistry*; D005434:Flow Cytometry; D015699:HIV Envelope Protein gp120 / Q000502:physiology*; D008722:Methods; D008856:Microscopy, Fluorescence; D011994:Recombinant Proteins / Q000494:pharmacology
D001425:Bacterial Outer Membrane Proteins; D015699:HIV Envelope Protein gp120; D011994:Recombinant Proteins; C063113:ice nucleation protein