Toxins from bacteria. EXS 2010;100:1-29
Date
04/03/2010Pubmed ID
20358680Pubmed Central ID
PMC3564551DOI
10.1007/978-3-7643-8338-1_1Scopus ID
2-s2.0-77950880789 (requires institutional sign-in at Scopus site) 86 CitationsAbstract
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.
Author List
Henkel JS, Baldwin MR, Barbieri JTAuthor
Joseph T. Barbieri PhD Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsBacteria
Bacterial Proteins
Bacterial Toxins
Botulinum Toxins
Enterotoxins
Humans
Models, Molecular
Pore Forming Cytotoxic Proteins
Protein Conformation
Structure-Activity Relationship
Virulence Factors
