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




 

Clin Diagn Lab Immunol. 1999 Jul;6(4):499-503. Unique Identifier :

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.

JOURNAL ARTICLE Bacterial Outer Membrane Proteins/*PHARMACOLOGY Blotting, Western Cell Separation Enzyme-Linked Immunosorbent Assay/METHODS Escherichia coli/*CHEMISTRY Flow Cytometry HIV Envelope Protein gp120/*PHYSIOLOGY Methods Microscopy, Fluorescence Recombinant Proteins/PHARMACOLOGY Support, Non-U.S. Gov't



 




Information in this article was accurate in November 30, 1999. The state of the art may have changed since the publication date. This material is designed to support, not replace, the relationship that exists between you and your doctor. Always discuss treatment options with a doctor who specializes in treating HIV.