Versatility of a vector for expressing foreign polypeptides at the surface of gram-negative bacteria.
A wide variety of peptides in terms of length and sequence can be expressed at the surface of the bacterium Escherichia coli by genetic insertion into a 'permissive' site of the outer membrane protein LamB, used as a carrier. The resulting hybrid proteins essentially keep their biological activities with inserts of up to about 60 amino acid residues, and of a large range of predicted structures or hydrophobicities. This reflects a remarkable flexibility in the organization of the protein, but also in the export machinery. The method used to select such a permissive site is quite general and its potential to generate applications, including a versatile type of live bacterial vaccine, are discussed.
Charbit
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A
CNRS-UA271, INSERM-U163, Unité de Programmation Moléculaire et Toxicologie Génétique, Institut Pasteur, France.
Molla
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A
Saurin
W
W
Hofnung
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D004251:DNA Transposable Elements; D005822:Genetic Vectors; D006090:Gram-Negative Bacteria / Q000235:genetics*; D006825:Hybridomas; D008969:Molecular Sequence Data; D009841:Oligonucleotides; D010455:Peptides / Q000235:genetics*; D010957:Plasmids
D004251:DNA Transposable Elements; D009841:Oligonucleotides; D010455:Peptides