EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia coli

EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia... Enteropathogenic Escherichia coli uses a type III secretion apparatus to deliver proteins essential for pathogenesis to the host epithelium. Several proteins have been detected in culture supernatants of the prototype EPEC strain E2348/69 and three of these, EspA, EspB, and EspD, use type III machinery for export. Here, we report the identification and characterization of CesD, a protein required for proper EspB and EspD secretion. CesD shows sequence homology to chaperone proteins from other type III secretion pathways. Based on this, we hypothesize that CesD may function as a secretion chaperone in EPEC. A mutation in cesD abolished EspD secretion into culture supernatants and reduced the amount of secreted EspB, but had little effect on the amount of secreted EspA. The mutant strain was negative for both FAS and Tir phosphorylation, consistent with the previously described roles for EspB and EspD in EPEC pathogenesis. CesD was shown to interact with EspD but not EspB or EspA. CesD was detected in the bacterial cytosol, and, surprisingly, a substantial amount of the protein was also found to be associated with the inner membrane. Thus, although CesD has some attributes that are similar to other type III secretion chaperones, its membrane localization separates it from previously described members of this family. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular Microbiology Wiley

EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia coli

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Publisher
Wiley
Copyright
Blackwell Science Ltd, Oxford
ISSN
0950-382X
eISSN
1365-2958
D.O.I.
10.1046/j.1365-2958.1998.00771.x
Publisher site
See Article on Publisher Site

Abstract

Enteropathogenic Escherichia coli uses a type III secretion apparatus to deliver proteins essential for pathogenesis to the host epithelium. Several proteins have been detected in culture supernatants of the prototype EPEC strain E2348/69 and three of these, EspA, EspB, and EspD, use type III machinery for export. Here, we report the identification and characterization of CesD, a protein required for proper EspB and EspD secretion. CesD shows sequence homology to chaperone proteins from other type III secretion pathways. Based on this, we hypothesize that CesD may function as a secretion chaperone in EPEC. A mutation in cesD abolished EspD secretion into culture supernatants and reduced the amount of secreted EspB, but had little effect on the amount of secreted EspA. The mutant strain was negative for both FAS and Tir phosphorylation, consistent with the previously described roles for EspB and EspD in EPEC pathogenesis. CesD was shown to interact with EspD but not EspB or EspA. CesD was detected in the bacterial cytosol, and, surprisingly, a substantial amount of the protein was also found to be associated with the inner membrane. Thus, although CesD has some attributes that are similar to other type III secretion chaperones, its membrane localization separates it from previously described members of this family.

Journal

Molecular MicrobiologyWiley

Published: Mar 1, 1998

References

  • A novel DnaJ‐like protein in Escherichia coli inserts into the cytoplasmic membrane with a type III topology
    Clarke, Clarke; Jacq, Jacq; Holland, Holland
  • The chaperone‐like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensable for targeting to the secretion loci
    Frithz‐Lindsten, Frithz‐Lindsten; Rosqvist, Rosqvist; Johansson, Johansson; Forsberg, Forsberg
  • EspA, a protein secreted by enteropathogenic Escherichia coli , is required to induce signals in epithelial cells
    Kenny, Kenny; Lai, Lai; Finlay, Finlay; Donnenberg, Donnenberg
  • Molecular chaperones and protein translocation across the Escherichia coli inner membrane
    Kumamoto, Kumamoto
  • A cloned pathogenicity island from enteropathogenic Escherichia coli confers the attaching and effacing phenotype on E. coli K‐12
    McDaniel, McDaniel; Kaper, Kaper
  • The hrp gene locus of Pseudomonas solanacearum , which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex
    Van Gijsegem, Van Gijsegem; Gough, Gough; Zischek, Zischek; Niqueux, Niqueux; Arlat, Arlat; Genin, Genin
  • SycE, a chaperone‐like protein of Yersinia enterocolitica involved in the secretion of YopE
    Wattiau, Wattiau; Cornelis, Cornelis
  • Customized secretion chaperones in pathogenic bacteria
    Wattiau, Wattiau; Woestyn, Woestyn; Cornelis, Cornelis
  • The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes
    Woestyn, Woestyn; Sory, Sory; Boland, Boland; Lequenne, Lequenne; Cornelis, Cornelis

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