Toxins from bacteria

  • James S. Henkel
  • Michael R. Baldwin
  • Joseph T. Barbieri
Part of the Experientia Supplementum book series (EXS, volume 100)


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.


Diphtheria Toxin Bacterial Toxin Bordetella Pertussis Botulinum Neurotoxin Translocation Domain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Birkhäuser Verlag/Switzerland 2010

Authors and Affiliations

  • James S. Henkel
    • 1
  • Michael R. Baldwin
    • 2
  • Joseph T. Barbieri
    • 1
  1. 1.Department of Microbiology and Molecular GeneticsMedical College of WisconsinMilwaukeeUSA
  2. 2.Department of Molecular Microbiology and ImmunologyUniversity of MissouriColumbiaUSA

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