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


Singh, MP; Shaw, RK; Knutton, S; Pallen, MJ; Crepin, VF; Frankel, G; (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. 2221-6. ISSN 0021-9193 DOI: https://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: Article
Faculty and Department: Faculty of Infectious and Tropical Diseases > Dept of Pathogen Molecular Biology
PubMed ID: 18178741
URI: http://researchonline.lshtm.ac.uk/id/eprint/4646440

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