Abstract
The large clostridial toxins (LCTs) are a group of homologous, high molecular weight proteins that include toxin A and toxin B from Clostridium difficile (TcdA and TcdB), the lethal and hemorrhagic toxins from C. sordellii (TcsL and TcsH), α-toxin from C. novyi (Tcnα), and a large cytotoxin from C. perfringens (TpeL). The LCTs share a glycosyltransferase enzymatic activity that results in the inactivation of specific Rho and Ras GTPases, essential signaling proteins and regulators within eukaryotic cells. The importance of these toxins in the context of disease has led many to apply structural and functional approaches to the understanding of LCT mechanism.
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Acknowledgments
Work in the Lacy laboratory is supported by United States Department of Veterans Affairs Award BX002943, Public Health Service grant AI095755 from the National Institutes of Health, and the Burroughs Wellcome Fund through an Investigators in the Pathogenesis of Infectious Disease Fellowship.
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Alvin, J.W., Lacy, D.B. (2018). Structure Function Studies of Large Clostridial Cytotoxins. In: Stiles, B., Alape-Girón, A., Dubreuil, J., Mandal, M. (eds) Microbial Toxins. Toxinology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6449-1_26
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DOI: https://doi.org/10.1007/978-94-007-6449-1_26
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