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Autoproteolytic activation of bacterial toxins Shen AToxins (Basel) 2010[May]; 2 (5): 963-77Protease 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 (InsP(6)), 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.|Bacterial Toxins/*metabolism[MESH]|Clostridium/metabolism/pathogenicity[MESH]|Cysteine Proteases/*metabolism[MESH]|Phytic Acid/metabolism[MESH]|Protein Conformation[MESH]|Vibrio cholerae/pathogenicity[MESH] |
