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Guidebook to Protein Toxins and Their Use in Cell Biology


Description: Many bacteria, animals, and plants produce toxins that can prove lethal to other organisms. Toxins are a form of "biological warfare" that helps their producer to survive and so confer an evolutionary advantage. They display an extraordinary range of complexity, from the formic acid provided by ants to bacterial proteins composed of thousands of amino acids. This Guidebook catalogues protein and peptide toxins, and will be of great interest to the cell biologist.

Toxins are produced by many prokaryotes, plants, and animals in an effort to gain an evolutionary advantage. They range in complexity from the ants formic acid to bacterial proteins composed of thousands of amino acids. Their use in cell research has been of major significance in many areas; this book considers the more complex toxins, calling on the expertise of a wide range of contributors. Particularly useful are the cellular schemes and the grouping of toxins in relation to their modes of action and cellular effects.

Topics covered include:
- membrane-permeabilizing toxins
- toxins affecting signal transduction and protein synthesis
cytoskeleton-affecting toxinsl- toxins affecting the immune and inflammatory response
- toxins affecting membrane traffic
- toxins that target sodium, potassium, and calcium channels, and the acetylcholine receptor
- ryanodine receptor toxins
- presynaptic toxins
- toxins targeting the glutamate receptor

Toxins are being used extensively in a variety of research disciplines including cell biology, neuroscience, and toxicology, and this volume will be an essential guide to many entering the field or those readers who need basic information about what specific toxins might contribute to their research.

About the Authors

Edited by Rino Rappuoli, IRIS, Chiron Vaccines Immunobiological Research Institute, Siena, Italy , and Cesare Montecucco, Centro CNR Biomembrane and Universita di Padova, Italy



Contents: List of Contributors
Preface

1. Membrane permeabilizing toxins
Introduction
J. Dufourcq- and S. Castano
Streptolysin (Streptococcus pyogenes)
S. Bhakdi,- M. Kehoe, A. Valeva, U. Weller,
and M. Palmer
Cholesterol binding toxins (Streptococcus,
Bacillus, Clostridium, Listeria)
J. Alouf
o-Toxin (Staphylococcus aureus)
G. Menestrina- and M. Ferreras)
5-Toxin (Staphylococcus aureus) and melittin
(Apis mellifera)
J. Dufourcq- and S. Castano
Aerolysin (Aeromonas hydrophila)
J.T.Buckley
Escherichia coli hemolysin
A. Ludwig and W. Goebel-

2. Toxins affecting signal transduction
Introduction
R. Rappuoli
Cholera toxin (Vibrio cholerae)
M. Pizza,- M. R. Fontana, and R. Rappuoli
Heat-labile enterotoxins (Escherichia coli)
R. K. Holmes
Pertussis toxin (Bordetella pertussis)
R. Rappuoli- and M. G. Pizza
Exoenzyme C3 (Clostridium botulinum)
E. Lemichez, P. Boquet, and M. R. Popoff-
Adenylate cyclase toxin (Bordetella sp.)
P. Sebo and A. Ullmann-
Anthrax edema factor (Bacillus anthracis)
S. H. Leppla

3. Toxins affecting protein synthesis
Introduction
J. R. Murphy
Diphtheria toxin (Corynebacterium diphtheriae)
J. R. Murphy
Pseudomonas aeruginosa exotoxin A
S. Olsnes
Shiga toxins (Shigella dysenteriae serotype I,
Escherichia coli)
A. R. Melton-Celsa- and A. OBrien
Ricin (Ricinus communis)
K. Sandvig
Ribosome-inactivating proteins
F. Stirpe
o-Sarcin and related toxins (Aspergillus)
M. Gasset

4. Cytoskeleton-affecting toxins
Introduction
K. Aktories
C2 toxin (Clostridium botulinum type C and D)
K. Aktories
Cytotoxic necrotizing factors (Escherichia coli)
G. Donelli- and C. Fiorentini
Enterotoxin A and cytotoxin B (Clostridium
difficile)
C. von Eichel-Streiber
ActA (Listeria monocytogenes)
C. Kocks and P. Cossart-
IcsA (Shigella flexneri)
C Egile and P. J. Sansonetti-
Zonula occludens toxin (Vibrio cholerae)
A. Fasano

5. Toxins affecting the immune and inflammatory response
ntroduction
J. Alouf
Pyrogenic exotoxins (superantigens)
(Staphylococcus aureus and Streptococcus
Pyogenes)
B. Fleischer
Anthrax lethal toxin (Bacillus anthracis)
P. C. Hanna and R. J. Collier-
Leukocidins and gamma lysins
(Staphylococcus so.)
M. Ferraras and G. Menestrina-

6. Toxins affecting membrane traffic
Introduction
C. Montecucco- and R. Rappuoli
Tetanus neurotoxin (Clostridium tetani)
R. Pellizzari and O. Rossetto-
VAMP-specific botulinum neurotoxins
G. Schiavo
Botulinum neurotoxins type A and E
(Clostridium botulinum)
O. Rossetto- and R. Pellizzari
Botulinum neurotoxin type C (Clostridium
botulinum)
J. Herreros and J. Blasi-
Vacuolating cytotoxin (Helicobacter pylori)
E. Papini and J. L Telford-

7. Sodium channel-targeted toxins
Introduction
J. A. Benson
o-Scorpion toxins
M.-F. Martin-Eauclaire- and P. E. Bougis
j3-Scorpion toxins
H. Rochat
Excitatory insect selective neurotoxins from
scorpion venoms
E. Zlotkin
Depressant insect selective neurotoxins from
scorpion venoms
E. Zlotkin
p-Conotoxins (Conus geographus)
L.J.Cruz
ju-Agatoxins (Agelenopsis aperta)
M. E. Adams- and T. M. Morris
Anthopleurin-A, -B, and -C (anemone toxin)
S. Shibata
Anemone toxins (type II)
R. S. Norton
Calitoxins
L. Cariello

8. Potassium channel-targeted toxins
Introduction
O. Pongs
Kaliotoxin
M.-F. Martin-Eauclaire
Scyllatoxin (Leiurus quinquestriatus hebraeus)
M. Hugues and M. Lazdunski-
Apamin (honey bee Apis mellifera)
H. Repp- and F. Dreyer
MCD peptide (honey bee Apis mellifera)
H. Repp- and F. Dreyer
Charybdotoxin and iberiotoxin (Leiurus
quinquestriatus var. hebraeus and Buthus
famulus)
M.L. Garcia
Margatoxin, noxiustoxin, and kaliotoxin
(Centruroides margaritatus, Centruroides
noxius, Androctonus mauretanicus)
R. Slaughter
Dendrotoxins (Dendroaspis species)
A.L.Harvey
Sea anemone potassium channel toxins
M. W. Pennington,- W. R. Kem, and E. Karlsson

9. Calcium channel-targeted toxins
Introduction
D. Pietrobon 1
o>-Conotoxins (Conus spp.)
B. M. Olivera,- J. S. Imperial, and D. Yoshikami
co-Agatoxins (Agelenopsis aperta)
T. M. Norris and M. E. Adams-
a>-Grammotoxin SIA (Grammostola spatulata
Chilean pink tarantula)
R. A. Lampe- and R. A. Keith
Hololena toxin (Hololena curta)
C. W. Bowers
PLTXII (Plectreurys tristes)
W. D. Branton
Calciseptine (Dendroaspis polylepis)
G. Romey, H. Schweitz, and M. Lazdunski-
Calcicludine (Dendroaspis angusticeps)
G. Romey, H. Schweitz, and M. Lazdunski-
/3-Leptinotarsin-h
P. Washbourne
Taicatoxin (Oxyuranus scutelatus scutelatus)
L. D. Possani

10. Acetylcholine receptor targeted toxins
Introduction
F. Clementi
o-Bungarotoxin (Bungarus multicinctus)
C. Gotti
o-Cobratoxin (Naja kaouthia)
A. Menez- and D. Servent
Erabutoxins (Laticauda semifasciata)
A. M6nez- and D. Servent
Toxin a (Naja nigricollis)
A. Menez
K-Bungarotoxin (Bungarus multicinctus)
V. Chiappinelli
a-Conotoxins (Conus spp.)
B. Olivers- and J. M. Mclntosh
Snake toxins against muscarinic acetylcholine
202 receptors
E. Karlsson-, M. Jolkkonen, and A. Aden

11. Ryanodine receptor toxins
Introduction
S. Treves and F. Zorzato-
Helothermine (Heloderma horridum horridum)
B. Becerril, L. Pardo, and L. D. Possani-

12. Presynaptic toxins
Introduction
C. Montecucco
Jb-Bungarotoxin (Bungarus multicinctus)
D. Mebs
Rattlesnake venom neurotoxins:
crotoxin-related proteins
A. L Bieber, C. Bon,- and G. Faure
Ammodytoxins (Vipera ammodytes ammodytes)
F. Gubensek- and I. Krizaj 2
Notexins (Notechis scutatus scutatus)
S. Gasparini and A. Menez-
Textilotoxin (Pseudonaja textilis textilis)
J. A. Pearson, D. Barnett, A. Comis, M. Connor,
B. M. Harrison, D. R. Lloyd, G. M. Nicholson,
P. Nicholson, K. V. Retson, I. Spence, M. I. Tyler,
H. I. Wilson, and M. E. M. Howden-
Taipoxin
J. B. Harris
a-Latrotoxin (black widow spider)
A. Malgaroli and J. Meldolesi-
a-Latroinsectotoxin (Latrodectus mactans
tredecimguttatus)
E. V. Grishin- and M. V. Khvotchev
Pardaxin (Pardachirus marmoratus)
E. Bloch-Shilderman, S. Abu-Raya, and
P. Lazarovici-
Palytoxin (Corals of the spp. Palythoa)
E. Habermann
Equinatoxins (Actinia equina L., sea anemone)
P. Macek

13. Glutamate receptor-targeted toxins
Introduction
C. Chiamulera and F. Ferraguti-
Conantokins (Conus spp.)
B. M. Olivera- and D. J. Steel
Index


Reviews: The authors have concisely compiled structure, function, and toxicity data for 78 protein toxins in a unique, accessible format that allows cell biologists to learn how protein toxins have aided in the dissection of cellular processes. --Journal of Chemical Education "Both our understanding of the actions of protein toxins and their uses as tools in cell biology have undergone an explosion in recent years. It almost seems that there is now a toxin to disrupt every aspect of cell metabolism. This volume is composed of short (1 to 3 page) summaries on the mechanism of action and uses of over 75 different protein toxins. It will be an invaluable reference for biological sciences and medical school libraries. Given the rapid pace of progress in this area, an additional attraction of this work is that updated information will be available on the World Wide Web."--The Quarterly Review of Biology


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