We have developed a system for expressing and displaying recombinant proteins, on the surface of Escherichia coli cells using the flagellin gene (hag). In order to produce fusion proteins, DNA fragments encoding a small peptide 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, green fluorescent protein (GFP) and a bacterial alkaline phosphatase (BAP), respectively were inserted into the dispensable D3 domain encoded by hag. Each 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 displayed in the flagellar fraction as fusion proteins. Although with lower efficiency, sFv, BAP and GFP could also be expressed in the flagellar fraction. Therefore, this system is useful for epitope analysis and with some improvements, the method could be useful for the expression of heterologous proteins on the cell surface.