TY  - JOUR
AB  - 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.
AU  - Weiss, André
AU  - Kortemeier, David
AU  - Brockmeyer, Jens
DA  - 2014-09-16
DO  - doi:10.3390/toxins6092719
KW  - EspPα
KW  - EspI
KW  - SPATE
KW  - virulence factor
KW  - EHEC
KW  - STEC
KW  - biochemical characterisation
KW  - substrate specificity
LA  - eng
N1  - Toxins 6 (2014) 9, 2719-2731
N1  - Finanziert durch den Open-Access-Publikationsfonds 2014/2015 der Deutschen Forschungsgemeinschaft (DFG) und der Westfälischen Wilhelms-Universität Münster (WWU Münster).
PY  - 2014-09-16
SN  - 2072-6651
TI  - Biochemical Characterization of the SPATE Members EspPα and EspI
UR  - https://nbn-resolving.org/urn:nbn:de:hbz:6-91319380992
Y2  - 2024-12-27T06:58:51
ER  -