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

Stuart Knutton, Man Rosenshine, Mark J. Pallen, Israel Nisan, Bianca C. Neves, Christopher Bain, Carmel Wolff, Gordon Dougan, Gad Frankel

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413 Citations (Scopus)


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 languageEnglish
Pages (from-to)2166-2176
Number of pages11
JournalThe EMBO Journal
Issue number8
Publication statusPublished - 15 Apr 1998
Externally publishedYes


  • EPEC
  • EspA
  • EspB
  • Protein translocation

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