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J. Bacteriol. doi:10.1128/JB.01753-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. 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

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 and Division of Immunity and Infection, School of Medicine, University of Birmingham, Birmingham B15 2TT, UK

* To whom correspondence should be addressed. Email: g.frankel{at}imperial.ac.uk.


  Abstract

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




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