S. Ezaki et al., Display of heterologous gene products on the Escherichia coli cell surfaceas fusion proteins with flagellin, J FERM BIOE, 86(5), 1998, pp. 500-503
We have developed a system for expressing and displaying recombinant protei
ns, on the surface of Escherichia coli cells using the flagellin gene (hag)
. In order to produce fusion proteins, DNA fragments encoding a small pepti
de with 15 amino acid residues (P15), the constant region of the antibody L
chain (region C), a single chain Fv (sFv) of an anti-porphyrin antibody, g
reen fluorescent protein (GFP) and a bacterial alkaline phosphatase (BAP),
respectively were inserted into the dispensable D3 domain encoded by hag. E
ach fusion gene was expressed in LS, coli YK4516, a strain that lacks hag.
The peptide linker P15 and the region C were efficiently expressed and disp
layed in the flagellar fraction as fusion proteins. Although with lower eff
iciency, sFv, BAP and GFP could also be expressed in the flagellar fraction
. Therefore, this system is useful for epitope analysis and with some impro
vements, the method could be useful for the expression of heterologous prot
eins on the cell surface.