Open AccessCell surface presentation of recombinant (poly‐) peptides including functional T‐cell epitopes by the AIDA autotransporter system
Author(s) -
Konieczny Marc P.J.,
Suhr Martin,
Noll Annette,
Autenrieth Ingo B.,
Alexander Schmidt M.
Publication year - 2000
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.2000.tb01446.x
Subject(s) - biology , epitope , bacterial adhesin , secretion , virulence , yersinia , microbiology and biotechnology , escherichia coli , bacterial outer membrane , groel , recombinant dna , yersinia enterocolitica , antigen presentation , protein subunit , antigen , bacteria , t cell , biochemistry , immune system , gene , genetics
For the efficient surface presentation and release of virulence factors especially pathogenic Gram‐negative bacteria have developed several distinct secretion mechanisms. An increasing number of pathogens in various species employs a mechanism denoted the ‘autotransporter’ pathway. This pathway is characterised by an outer membrane translocator module representing the C‐terminal domain of the transported protein itself. An intriguing potential application of such systems involves the transport and surface expression of recombinant proteins or peptides, like e.g. the presentation of antigens for the generation of live oral vectors as vaccine carriers. Here we report on 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 coli (LTB) as well as of functional T‐cell epitopes of Yersinia enterocolitica heat‐shock protein 60 (Y‐hsp60) on the surface of E. coli .