Premium
A novel EspA‐associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells
Author(s) -
Knutton Stuart,
Rosenshine Ilan,
Pallen Mark J.,
Nisan Israel,
Neves Bianca C.,
Bain Christopher,
Wolff Carmel,
Dougan Gordon,
Frankel Gad
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.8.2166
Subject(s) - biology , escherichia coli , enteropathogenic escherichia coli , organelle , chromosomal translocation , microbiology and biotechnology , escherichia coli proteins , bacterial protein , bacteria , biochemistry , gene , genetics
Enteropathogenic Escherichia coli (EPEC), like many bacterial pathogens, employ a type III secretion system to deliver effector proteins across the bacterial cell. In EPEC, four proteins are known to be exported by a type III secretion system—EspA, EspB and EspD required for subversion of host cell signal transduction pathways and a translocated intimin receptor (Tir) protein (formerly Hp90) which is tyrosine‐phosphorylated following transfer to the host cell to become a receptor for intimin‐mediated intimate attachment and ‘attaching and effacing’ (A/E) lesion formation. The structural basis for protein translocation has yet to be fully elucidated for any type III secretion system. Here, we describe a novel EspA‐containing filamentous organelle that is present on the bacterial surface during the early stage of A/E lesion formation, forms a physical bridge between the bacterium and the infected eukaryotic cell surface and is required for the translocation of EspB into infected epithelial cells.