title: Autoproteolytic activation of bacterial toxins.
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 (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.
authors: Department of Pathology, Stanford School of Medicine, 300 Pasteur Drive, Stanford, California, USA. ashen2@stanford.edu
authors: Aimee
authors: A
authors: Shen
mesh_terms: D001427:Bacterial Toxins / Q000378:metabolism*; D003013:Clostridium / Q000378:metabolism / Q000472:pathogenicity; D057056:Cysteine Proteases / Q000378:metabolism*; D010833:Phytic Acid / Q000378:metabolism; D011487:Protein Conformation; D014734:Vibrio cholerae / Q000472:pathogenicity
chemical_list: D001427:Bacterial Toxins; C434464:RtxA protein, Vibrio cholerae; D010833:Phytic Acid; D057056:Cysteine Proteases