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Journal of Bacteriology, March 2008, p. 2221-2226, Vol. 190, No. 6
0021-9193/08/$08.00+0     doi:10.1128/JB.01753-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Identification of Amino Acid Residues within the N-Terminal Domain of EspA That Play a Role in EspA Filament Biogenesis and Function{triangledown}

Mona P. Singh, Robert K. Shaw, Stuart Knutton, Mark J. Pallen, Valerie F. Crepin, and Gad Frankel*

Division of Cell and Molecular Biology, Imperial College, London SW7 2AZ, United Kingdom, and Division of Immunity and Infection, School of Medicine, University of Birmingham, Birmingham B15 2TT, United Kingdom

Received 1 November 2007/ Accepted 23 December 2007

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.

* Corresponding author. Mailing address: Division of Molecular and Cellular Biology, Flowers Building, Imperial College London, London SW7 2AZ, United Kingdom. Phone: 44 020 2594 5253. Fax: 44 020 5794 3069. E-mail: g.frankel{at}imperial.ac.uk

{triangledown} Published ahead of print on 4 January 2008.

Journal of Bacteriology, March 2008, p. 2221-2226, Vol. 190, No. 6
0021-9193/08/$08.00+0     doi:10.1128/JB.01753-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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