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

被引:39
作者
Konieczny, MPJ
Suhr, M
Noll, A
Autenrieth, IB
Schmidt, MA
机构
[1] Univ Munster, Zentrum Mol Biol Entzundung, Inst Infektiol, D-48149 Munster, Germany
[2] Max Von Pettenkofer Inst Hyg & Med Microbiol, D-80336 Munich, Germany
来源
FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY | 2000年 / 27卷 / 04期
关键词
adhesin-involved-in-diffuse-adherence (AIDA) autotransporter; bacterial carrier; surface presentation; heat labile enterotoxin (LTB); Escherichia coli; Escherichia coli NISSLE 1917; Yersinia enterocolitica hsp60 T-cell epitopes;
D O I
10.1016/S0928-8244(99)00210-2
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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 All 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 heal-shock protein 60 (Y-hsp60) on the surface of E. coli. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:321 / 332
页数:12
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