Abstract
Large clostridial cytotoxins are produced by Clostridium difficile, Clostridium sordellii, Clostridium novyi, and Clostridium perfringens. The protein toxins are major pathogenic factors and causally involved in various diseases induced by Clostridia. The molecular mechanism of the toxins is the inactivation of GTP-binding proteins of Rho and Ras subfamilies, which act as molecular switches in various essential cellular processes. The toxins share a common multidomain architecture, which is characterized by an ABCD model. The structure consists of the N-terminal domain A with glycosyltransferase activity, the C-terminal receptor binding domain B, the cutting domain C with an inositol hexakisphosphate (InsP6)–activated auto-proteolytic cysteine protease, and the delivery domain D, which is involved in translocation of part of the toxins into the cytosol.
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