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

MP Singh; Robert Shaw; Stuart Knutton; Mark Pallen; VF Crepin; G Frankel

doi:10.1128/JB.01753-07

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

MP Singh
, Robert Shaw
, Stuart Knutton
, Mark Pallen
, VF Crepin
, G Frankel

Biosciences

Research output: Contribution to journal › Article

7 Citations (Scopus)

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.

Original language	English
Pages (from-to)	2221-2226
Number of pages	6
Journal	Journal of Bacteriology
Volume	190
Issue number	6
Early online date	4 Jan 2008
DOIs	https://doi.org/10.1128/JB.01753-07
Publication status	Published - 4 Jan 2008

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10.1128/JB.01753-07

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title = "Identification of Amino Acid Residues within the N-Terminal Domain of EspA That Play a Role in EspA Filament Biogenesis and Function",

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.",

author = "MP Singh and Robert Shaw and Stuart Knutton and Mark Pallen and VF Crepin and G Frankel",

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AU - Singh, MP

AU - Shaw, Robert

AU - Knutton, Stuart

AU - Pallen, Mark

AU - Crepin, VF

AU - Frankel, G

PY - 2008/1/4

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N2 - 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.

AB - 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.

U2 - 10.1128/JB.01753-07

DO - 10.1128/JB.01753-07

M3 - Article

C2 - 18178741

VL - 190

SP - 2221

EP - 2226

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 6

ER -

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

Abstract

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