A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells

The EMBO Journal
S KnuttonG Frankel

Abstract

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.

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Citations

Aug 26, 1998·Folia Microbiologica·I NisanI Rosenshine
Jun 1, 2005·Journal of Molecular Biology·Valérie F CrepinGad Frankel
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