Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Display of Proteins on the Surface of Escherichia coli by C-Terminal Deletion Fusion to the Salmonella typhimurium OmpC

  • CHOI JONG-HYUN (Metabolic and Biomolecular Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering) ;
  • CHOI, JONG-IL (Metabolic and Biomolecular Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering) ;
  • LEE, SANG-YUP (Metabolic and Biomolecular Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering, Department of BioSystems and Bioinformatics Research Center, Korea Advanced Institute of Science and Technology)
  • Published : 2005.02.01
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Abstract

A new system for displaying proteins on the surface of Escherichia coli was developed using the Salmonella typhimurium outer membrane protein C (OmpC) as an anchoring motif. The C-terminal deletionfusion strategy was developed to fuse the polyhistidine peptides and green fluorescent protein (GFP) to the Cterminal of the truncated functional portion of OmpC. The polyhistidine peptides of up to 243 amino acids could besuccessfully displayed on the E. coli cell surface, which allowed recombinant E. coli to adsorb up to 34.2 μmol of Cd2+ per gram dry cell weight. The GFP could also be successfully displayed on the E. coli cell surface. These results suggest that the C-terminal deletion-fusion strategy employing the S. typhimurium OmpC as an anchoring motif provides a new efficient way for the display of large proteins on the surface of E. coli.

Keywords

References

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