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Toxins from bacteria

  • Chapter
Molecular, Clinical and Environmental Toxicology

Part of the book series: Experientia Supplementum ((EXS,volume 100))

Abstract

Bacterial toxins damage the host at the site of bacterial infection or distant from the site. Bacterial toxins can be single proteins or oligomeric protein complexes that are organized with distinct AB structure-function properties. The A domain encodes a catalytic activity. ADP ribosylation of host proteins is the earliest post-translational modification determined to be performed by bacterial toxins; other modifications include glucosylation and proteolysis. Bacterial toxins also catalyze the non-covalent modification of host protein function or can modify host cell properties through direct protein-protein interactions. The B domain includes two functional domains: a receptor-binding domain, which defines the tropism of a toxin for a cell and a translocation domain that delivers the A domain across a lipid bilayer, either on the plasma membrane or the endosome. Bacterial toxins are often characterized based upon the secretion mechanism that delivers the toxin out of the bacterium, termed types I–VII. This review summarizes the major families of bacterial toxins and also describes the specific structure-function properties of the botulinum neurotoxins.

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  1. Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI, 53151, USA

    James S. Henkel & Joseph T. Barbieri

  2. Department of Molecular Microbiology and Immunology, University of Missouri, M616 Medical Sciences Building, Columbia, MO, 65212, USA

    Michael R. Baldwin

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    Andreas Luch

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Henkel, J.S., Baldwin, M.R., Barbieri, J.T. (2010). Toxins from bacteria. In: Luch, A. (eds) Molecular, Clinical and Environmental Toxicology. Experientia Supplementum, vol 100. Birkhäuser Basel. https://doi.org/10.1007/978-3-7643-8338-1_1

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