Mechanisms of the cytopathic action of actin-ADP-ribosylating toxins
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چکیده
منابع مشابه
Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile
26 Some hypervirulent strains of Clostridium difficile produce the binary actin-ADP-ribosylating 27 toxin CDT in addition to the Rho-glucosylating toxins A and B. It has been suggested that the 28 presence of CDT increases the severity of the C. difficile-associated diseases including 29 pseudomembranous colitis. CDT contains a binding and translocation component CDTb, which 30 mediates the tra...
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Among the several toxins used by pathogenic bacteria to target eukaryotic host cells, proteins that exert ADP-ribosylation activity represent a large and studied family of dangerous and potentially lethal toxins. These proteins alter cell physiology catalyzing the transfer of the ADP-ribose unit from NAD to cellular proteins involved in key metabolic pathways. In the present study, we tested th...
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umber of clostridial bacteria produce toxins which ADP-ribosylate monomeric actin. These include botulinum C2 toxin (2), Clostridiumperfringens iota toxin (23, 26), Clostridium spiroforme toxin (20, 27), and an ADP-ribosyltransferase produced by Clostridium difficile (21). The toxins have turned out to be valuable tools for investigating the actin cytoskeleton since ADP-ribosylation of actin bl...
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ADP-ribosyltransferases (ADP-RTs) are a family of enzymes secreted by pathogenic bacteria. They catalyse the hydrolysis of NAD+ and the transfer of the ADPribosyl group onto specific target proteins [1,2]. Figure 1 Although ADP-RTs are important drug targets, only few inhibitors are known so far. The high selectivity of these inhibitors suggest different mechanism of binding to the ADP-RTs acti...
متن کاملADP-ribosylation of gelsolin-actin complexes by clostridial toxins.
ADP-ribosylation of the 1:1 (G-A) and 1:2 (G-A-A) gelsolin-actin complexes by Clostridium perfringens iota toxin and Clostridium botulinum C2 toxin was studied. Iota toxin ADP-ribosylated actin in the G-A complex from human platelets as effectively as skeletal muscle actin. The Km for NAD (4 microM) was identical for both substrates. C2 toxin ADP-ribosylated actin in the G-A complex with lower ...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 1992
ISSN: 0950-382X,1365-2958
DOI: 10.1111/j.1365-2958.1992.tb01749.x