Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif.
A novel cell surface display system was developed by employing Escherichia coli outer membrane protein C (OmpC) as an anchoring motif. Polyhistidine peptides consisting of up to 162 amino acids could be successfully displayed on the seventh exposed loop of OmpC. Recombinant cells displaying polyhistidine could adsorb up to 32.0 micromol of Cd(2+) per g (dry weight) of cells.
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Department of Chemical Engineering and BioProcess Engineering Research Center, Korea Advanced Institute of Science and Technology, Yusong-gu, Taejon 305-701, Korea.
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D000327:Adsorption; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D001483:Base Sequence; D001665:Binding Sites; D002104:Cadmium / Q000378:metabolism*; D002462:Cell Membrane / Q000502:physiology* / Q000648:ultrastructure; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D006639:Histidine; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019151:Peptide Library; D010455:Peptides / Q000032:analysis*; D018272:Porins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D015183:Restriction Mapping; D012685:Sepharose
C113724:OmpC protein; D019151:Peptide Library; D010455:Peptides; D018272:Porins; D011994:Recombinant Proteins; D002104:Cadmium; C033223:polyhistidine; D006639:Histidine; D012685:Sepharose