ADP-Ribosylating Toxins

1. Front Matter

   Pages I-X

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2. Entry of ADP-Ribosylating Toxins into Cells

   • I. H. Madshus, H. Stenmark

   Pages 1-26

3. Diphtheria Toxin and Pseudomonas aeruginosa Exotoxin A: Active-Site Structure and Enzymic Mechanism

   • B. A. Wilson, R. J. Collier

   Pages 27-41

4. Enhancement of Cholera Toxin-Catalyzed ADP-Ribosylation by Guanine Nucleotide-Binding Proteins

   • I. M. Serventi, J. Moss, M. Vaughan

   Pages 43-67

5. ADP-Ribosylation of Signal-Transducing Guanine Nucleotide-Binding Proteins by Pertussis Toxin

   • P. Gierschik

   Pages 69-96

6. Clostridial Actin-ADP-Ribosylating Toxins

   • K. Aktories, M. Wille, I. Just

   Pages 97-113

7. Clostridium botulinum C3 ADP-Ribosyltransferase

   • K. Aktories, C. Mohr, G. Koch

   Pages 115-131

8. Pseudomonas aeruginosa Exoenzyme S

   • J. Coburn

   Pages 133-143

9. Back Matter

   Pages 145-150

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ADP-ribosylating toxins have been the focus of intensive research for more than 30 years. Researchers from diverse fields of science have taken an interest in these bacterial toxins; they are studied, for example, by microbiologists, biochemists, cell biologists, and pharmacologists. There are two principal reasons for the broad and still growing interest in ADP­ ribosylating toxins. First, insights into the structure and functions of the toxins might be the key to prevention and treatment of diseases caused by the toxin-producing infectious micro­ organisms. Second, the ADP-ribosylating toxins provide potent and often unique pharmacological tools for the study of the physiological functions of their target proteins. The latter is especially the case with cholera and pertussis toxins, which both modify the IX-subunits of heterotrimeric G-proteins involved in signal transduction pathways. These toxins have proved invaluable in extending our basic understanding of the regulation of hormone-controlled signal transduction. This volume provides a review and an update of recent studies on the basic properties of bacterial ADP-ribosylating tbxins and/or exoenzymes. Our current knowledge of the cel­ lular entry mechanisms of ADP-ribosylating toxins is reviewed by MADSHUS and STENMARK. WILSON and COLLIER then deal with recent insights into the enzyme mechanism and active site structure of diphtheria toxin and Pseudomonas aeruginosa exotoxin A, which modify elongation factor 2. Toxins which ADP-ribosylate heterotrimeric G-proteins involved in trans­ membrane signal transduction are the subject of the next two chapters.

• GTP-bindende
• Proteine
• Toxin, Cholera
• Toxin, Diphterie-
• Toxin, Pertussis-
• Toxine, bakterielle
• bacteria
• protein
• proteins
• pseudomonas
• toxin

• Institut für Pharmakologie und Toxikologie, Universität des Saarlands, Homburg/saar, Germany

  Klaus Aktories

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