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Clinical and Diagnostic Laboratory Immunology, July 1999, p. 499-503, Vol. 6, No. 4
Department of Biotechnology, College of
Engineering and Bioproduct Research Center, Yonsei University, 134 Shinchon-Dong, Sudaemun-Ku, Seoul 120-749, Korea
Received 21 September 1998/Returned for modification 6 February
1999/Accepted 8 April 1999
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.
1071-412X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Cell Surface Display of Human Immunodeficiency
Virus Type 1 gp120 on Escherichia coli by Using Ice
Nucleation Protein
*
Corresponding author. Mailing address: Department of
Biotechnology, College of Engineering and Bioproduct Research Center, Yonsei University, 134 Shinchon-Dong, Sudaemun-Ku, Seoul, 120-749, Korea. Phone: 82-2-361-2887. Fax: 82-2-362-7265. E-mail:
skyoo{at}bubble.yonsei.ac.kr.
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