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Cell surface display of human immunodeficiency virus type 1 gp120 on Escherichia coli by using ice nucleation protein.


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 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.

SUBMITTER: Kwak YD 

PROVIDER: S-EPMC95715 | biostudies-literature | 1999 Jul

REPOSITORIES: biostudies-literature

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Cell surface display of human immunodeficiency virus type 1 gp120 on Escherichia coli by using ice nucleation protein.

Kwak Y D YD   Yoo S K SK   Kim E J EJ  

Clinical and diagnostic laboratory immunology 19990701 4


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 confirme  ...[more]

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