Bilingual day care in Zurich Kinderkrippe Zürich
Kinderbetreuung in Zürich Kinderkrippe Zürich
Kita in Zürich Kinderkrippe Zürich
Kinderkrippe in Zürich Seebach Kinderkrippe Seebach
Academic Journals Database
disseminating
quality controlled scientific knowledge



Autoproteolytic Activation of Bacterial Toxins

Author(s): Aimee Shen

Journal: Toxins ISSN 2072-6651
Volume: 2; Issue: 5; Start page: 963; Date: 2010;
Original page

Keywords: cysteine protease domain (CPD) | MARTX toxin | glucosylating toxin (GT) | inositol hexakisphosphate (InsP6) | glucosyltransferase (Glc) | structure activity relationship (SAR)

ABSTRACT
Protease domains within toxins typically act as the primary effector domain within target cells. By contrast, the primary function of the cysteine protease domain (CPD) in Multifunctional Autoprocessing RTX-like (MARTX) and Clostridium sp. glucosylating toxin families is to proteolytically cleave the toxin and release its cognate effector domains. The CPD becomes activated upon binding to the eukaryotic-specific small molecule, inositol hexakisphosphate (InsP6), which is found abundantly in the eukaryotic cytosol. This property allows the CPD to spatially and temporally regulate toxin activation, making it a prime candidate for developing anti-toxin therapeutics. In this review, we summarize recent findings related to defining the regulation of toxin function by the CPD and the development of inhibitors to prevent CPD-mediated activation of bacterial toxins.