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When Escherichia coli doesn't fit the mold: A pertussis-like toxin with altered specificity.


ABSTRACT: Bacterial toxins introduce protein modifications such as ADP-ribosylation to manipulate host cell signaling and physiology. Several general mechanisms for toxin function have been established, but the extent to which previously uncharacterized toxins utilize these mechanisms is unknown. A study of an Escherichia coli pertussis-like toxin demonstrates that this protein acts on a known toxin substrate but displays distinct and dual chemoselectivity, suggesting this E. coli pertussis-like toxin may serve as a unique tool to study G-protein signaling in eukaryotic cells.

SUBMITTER: Chen C 

PROVIDER: S-EPMC5592690 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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When <i>Escherichia coli</i> doesn't fit the mold: A pertussis-like toxin with altered specificity.

Chen Chen C   Barbieri Joseph T JT  

The Journal of biological chemistry 20170901 36


Bacterial toxins introduce protein modifications such as ADP-ribosylation to manipulate host cell signaling and physiology. Several general mechanisms for toxin function have been established, but the extent to which previously uncharacterized toxins utilize these mechanisms is unknown. A study of an <i>Escherichia coli</i> pertussis-like toxin demonstrates that this protein acts on a known toxin substrate but displays distinct and dual chemoselectivity, suggesting this <i>E. coli</i> pertussis-  ...[more]

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