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Toxins 2014, 6(9), 2719-2731; doi:10.3390/toxins6092719

Biochemical Characterization of the SPATE Members EspPα and EspI

Institute of Food Chemistry, Corrensstraße 45, 48149 Münster, Germany
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Received: 3 July 2014 / Revised: 18 August 2014 / Accepted: 21 August 2014 / Published: 16 September 2014
(This article belongs to the Section Bacterial Toxins)
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Abstract

The activity of serine proteases is influenced by their substrate specificity as well as by the physicochemical conditions. Here, we present the characterization of key biochemical features of the two SPATE members EspPα and EspI from Shiga-toxin producing Escherichia coli (STEC) and enterohemorrhagic E. coli (EHEC). Both proteases show high activity at conditions mimicking the human blood stream. Optimal activities were observed at slightly alkaline pH and low millimolar concentrations of the divalent cations Ca2+ and Mg2+ at physiological temperatures indicating a function in the human host. Furthermore, we provide the first cleavage profile for EspI demonstrating pronounced specificity of this protease. View Full-Text
Keywords: EspPα; EspI; SPATE; virulence factor; EHEC; STEC; biochemical characterisation; substrate specificity EspPα; EspI; SPATE; virulence factor; EHEC; STEC; biochemical characterisation; substrate specificity
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Weiss, A.; Kortemeier, D.; Brockmeyer, J. Biochemical Characterization of the SPATE Members EspPα and EspI. Toxins 2014, 6, 2719-2731.

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