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

Research output: Contribution to journalArticleResearchpeer-review

441 Citations (Scopus)

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 languageEnglish
Pages (from-to)2166-2176
Number of pages11
JournalEMBO Journal
Volume17
Issue number8
DOIs
Publication statusPublished - 15 Apr 1998
Externally publishedYes

Keywords

  • EPEC
  • EspA
  • EspB
  • Protein translocation

Cite this

Knutton, S., Rosenshine, M., Pallen, M. J., Nisan, I., Neves, B. C., Bain, C., ... Frankel, G. (1998). A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO Journal, 17(8), 2166-2176. https://doi.org/10.1093/emboj/17.8.2166
Knutton, Stuart ; Rosenshine, Man ; Pallen, Mark J. ; Nisan, Israel ; Neves, Bianca C. ; Bain, Christopher ; Wolff, Carmel ; Dougan, Gordon ; Frankel, Gad. / A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. In: EMBO Journal. 1998 ; Vol. 17, No. 8. pp. 2166-2176.
@article{4d389ec77ac74aef968de60aeb6ff45c,
title = "A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells",
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.",
keywords = "EPEC, EspA, EspB, Protein translocation",
author = "Stuart Knutton and Man Rosenshine and Pallen, {Mark J.} and Israel Nisan and Neves, {Bianca C.} and Christopher Bain and Carmel Wolff and Gordon Dougan and Gad Frankel",
year = "1998",
month = "4",
day = "15",
doi = "10.1093/emboj/17.8.2166",
language = "English",
volume = "17",
pages = "2166--2176",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "John Wiley & Sons",
number = "8",

}

Knutton, S, Rosenshine, M, Pallen, MJ, Nisan, I, Neves, BC, Bain, C, Wolff, C, Dougan, G & Frankel, G 1998, 'A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells', EMBO Journal, vol. 17, no. 8, pp. 2166-2176. https://doi.org/10.1093/emboj/17.8.2166

A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. / Knutton, Stuart; Rosenshine, Man; Pallen, Mark J.; Nisan, Israel; Neves, Bianca C.; Bain, Christopher; Wolff, Carmel; Dougan, Gordon; Frankel, Gad.

In: EMBO Journal, Vol. 17, No. 8, 15.04.1998, p. 2166-2176.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells

AU - Knutton, Stuart

AU - Rosenshine, Man

AU - Pallen, Mark J.

AU - Nisan, Israel

AU - Neves, Bianca C.

AU - Bain, Christopher

AU - Wolff, Carmel

AU - Dougan, Gordon

AU - Frankel, Gad

PY - 1998/4/15

Y1 - 1998/4/15

N2 - 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.

AB - 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.

KW - EPEC

KW - EspA

KW - EspB

KW - Protein translocation

UR - http://www.scopus.com/inward/record.url?scp=0032522344&partnerID=8YFLogxK

U2 - 10.1093/emboj/17.8.2166

DO - 10.1093/emboj/17.8.2166

M3 - Article

VL - 17

SP - 2166

EP - 2176

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 8

ER -