Display of proteins on the surface of Escherichia coli by C-terminal deletion fusion to the Salmonella typhimurium OmpC

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 deletion-fusion strategy was developed to fuse the polyhistidine peptides and green fluorescent protein (GFP) to the C-terminal of the truncated functional portion of OmpC. The polyhistidine peptides of up to 243 amino acids could be successfully displayed on the E. coli cell surface, which allowed recombinant E. coli to adsorb up to 34.2 mumol 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.