The filamentous type III secretion translocon of enteropathogenic Escherichia coli

Sarah J. Daniell, Noriko Takahashi, Rebecca Wilson, Devorah Friedberg, Ilan Rosenshine, Frank P. Booy, Robert K. Shaw, Stuart Knutton, Gad Frankel*, Shin Ichi Aizawa

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

120 Scopus citations


Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system (TTSS) to inject effector proteins into the plasma membrane and cytosol of infected cells. To translocate proteins, EPEC, like Salmonella and Shigella, is believed to assemble a macromolecular complex (type III secreton) that spans both bacterial membranes and has a short needle-like projection. However, there is a special interest in studying the EPEC TTSS owing to the fact that one of the secreted proteins, EspA, is assembled into a unique filamentous structure also required for protein translocation. In this report we present electron micrographs of EspA filaments which reveal a regular segmented substructure. Recently we have shown that deletion of the putative structural needle protein, EscF, abolished protein secretion and formation of EspA filaments. Moreover, we demonstrated that EspA can bind directly to EscF, suggesting that EspA filaments are physically linked to the EPEC needle complex. In this paper we provide direct evidence for the association between an EPEC bacterial membrane needle complex and EspA filaments, defining a new class of filamentous TTSS.

Original languageAmerican English
Pages (from-to)865-871
Number of pages7
JournalCellular Microbiology
Issue number12
StatePublished - 2001


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