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Identification of amino acid residues within the n-terminal domain of EspA that play a role in EspA filament biogenesis and function

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Singh, M. P., Shaw, Robert K., Knutton, S., Pallen, Mark J., Crepin, Valerie F. and Frankel, Gad (2008) Identification of amino acid residues within the n-terminal domain of EspA that play a role in EspA filament biogenesis and function. Journal of Bacteriology, 190 (6). pp. 2221-2226. doi:10.1128/JB.01753-07

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Official URL: http://dx.doi.org/10.1128/JB.01753-07

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Abstract

Enteropathogenic Escherichia coli employs a filamentous type III secretion system, made by homopolymerization of the translocator protein EspA. In this study, we have shown that the N-terminal region of EspA has a role in EspA's protein stability, interaction with the CesAB chaperone, and filament biogenesis and function.

Item Type: Journal Article
Divisions: Faculty of Medicine > Warwick Medical School > Biomedical Sciences > Microbiology & Infection
Faculty of Medicine > Warwick Medical School
Journal or Publication Title: Journal of Bacteriology
Publisher: American Society for Microbiology
ISSN: 0021-9193
Official Date: 2008
Dates:
DateEvent
2008Published
Volume: 190
Number: 6
Page Range: pp. 2221-2226
DOI: 10.1128/JB.01753-07
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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