Cell surface presentation of recombinant (poly-) peptides including functional T-cell epitopes by the AIDA autotransporter system

For the efficient surface presentation and release of virulence factors esp ecially pathogenic Gram-negative bacteria have developed several distinct s ecretion mechanisms. An increasing number of pathogens in various species e mploys a mechanism denoted the 'autotransporter' pathway. This pathway is c haracterised by an outer membrane translocator module representing the C-te rminal domain of the transported protein itself All intriguing potential ap plication of such systems involves the transport and surface expression of recombinant proteins or peptides, like e.g. the presentation of antigens fo r the generation of live oral vectors as vaccine carriers. Here we report o n the incorporation of heterologous (poly-) peptides in permissive sites of the translocator module of the adhesin-involved-in-diffuse-adherence (AIDA ) autotransporter system. We demonstrate the presentation of the B subunit of the heat labile enterotoxin of Escherichia coil (LTB) as well as of func tional T-cell epitopes of Yersinia enterocolitica heal-shock protein 60 (Y- hsp60) on the surface of E. coli. (C) 2000 Federation of European Microbiol ogical Societies. Published by Elsevier Science B.V. All rights reserved.