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.
Original language | English |
---|---|
Pages (from-to) | 2166-2176 |
Number of pages | 11 |
Journal | The EMBO Journal |
Volume | 17 |
Issue number | 8 |
DOIs | |
Publication status | Published - 15 Apr 1998 |
Externally published | Yes |
Keywords
- EPEC
- EspA
- EspB
- Protein translocation