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J. Microbiol. Biotechnol. 2005; 15(1): 141-146

Published online February 28, 2005

Copyright © The Korean Society for Microbiology and Biotechnology.

Display of Proteins on the Surface of Escherichia coli by C-Terminal Deletion Fusion to the Salmonella typhimurium OmpC

Jong Hyun Choi , Jong Il Choi and Sang Yup Lee 1*

Metabolic and Biomolecular Engineering National Research Laboratory Department of Chemical and Biomolecular EngineeringBioProcess Engineering Research Center and Center for Ultramicrochemical Process Systems Korea Advanced Institute ofScience and Technolo, 1Department of BioSystems and Bioinformatics Research Center Korea Advanced Institute of Science and Technology 373-1Guseong-dong Yuseong-gu Daejeon 305-701 Korea

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: Cellsurfacedisplay, SalmonellaOmpC, anchoringmotif, polyhistidine, GFP