H. Barth, K. Aktories, M. Popoff, and B. Stiles, Binary Bacterial Toxins: Biochemistry, Biology, and Applications of Common Clostridium and Bacillus Proteins, Microbiology and Molecular Biology Reviews, vol.68, issue.3, pp.373-402, 2004.
DOI : 10.1128/MMBR.68.3.373-402.2004

URL : http://mmbr.asm.org/content/68/3/373.full.pdf

I. Ohishi and Y. Odagiri, Histopathological effect of botulinum C2 toxin on mouse intestines, Infect Immun, vol.43, pp.54-58, 1984.

I. Ohishi, M. Iwasaki, and G. Sakaguchi, Purification and characterization of two components of botulinum C2 toxin, Infect Immun, vol.30, pp.668-673, 1980.

I. Ohishi, Response of mouse intestinal loop to botulinum C2 toxin: enterotoxic activity induced by cooperation of nonlinked protein components, Infect Immun, vol.40, pp.691-695, 1983.

I. Ohishi, Lethal and vascular permeability activities of botulinum C2 toxin induced by separate injections of the two toxin components, Infect Immun, vol.40, pp.336-339, 1983.

W. Wiegers, I. Just, H. Müller, A. Hellwig, and P. Traub, Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase, Eur J Cell Biol, vol.54, pp.237-245, 1991.

B. Stiles and T. Wilkins, Purification and characterization of Clostridium perfringens iota toxin: dependence on two nonlinked proteins for biological activity, Infect Immun, vol.54, pp.683-688, 1986.

J. Vandekerckhove, B. Schering, M. Bä-rmann, and K. Aktories, iota toxin ADP-ribosylates skeletal muscle actin in Arg-177, FEBS Letters, vol.75, issue.1-2, pp.48-52, 1987.
DOI : 10.1073/pnas.75.3.1106

URL : http://onlinelibrary.wiley.com/doi/10.1016/0014-5793(87)81129-8/pdf

S. Perelle, M. Gibert, P. Bourlioux, G. Corthier, and M. Popoff, Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196, Infect Immun, vol.65, pp.1402-1407, 1997.

M. Popoff, E. Rubin, D. Gill, and P. Boquet, Actin-specific ADPribosyltransferase produced by a Clostridium difficile strain, Infect Immun, vol.56, pp.2299-2306, 1988.

I. Gülke, G. Pfeifer, J. Liese, M. Fritz, and F. Hofmann, Characterization of the Enzymatic Component of the ADP-Ribosyltransferase Toxin CDTa from Clostridium difficile, Infection and Immunity, vol.69, issue.10, pp.6004-6011, 2001.
DOI : 10.1128/IAI.69.10.6004-6011.2001

M. Popoff and P. Boquet, Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin, Biochemical and Biophysical Research Communications, vol.152, issue.3, pp.1361-1368, 1988.
DOI : 10.1016/S0006-291X(88)80435-2

K. Aktories, M. Bärmann, I. Ohishi, S. Tsuyama, and K. Jakobs, Botulinum C2 toxin ADP-ribosylates actin, Nature, vol.85, issue.6077, pp.390-392, 1986.
DOI : 10.1038/322390a0

J. Vandekerckhove, B. Schering, M. Bä-rmann, and K. Aktories, Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in arginine 177, J Biol Chem, vol.263, pp.696-700, 1988.

A. Wegner and K. Aktories, ADP-ribosylated actin caps the barbed ends of actin filaments, J Biol Chem, vol.263, pp.13739-13742, 1988.

K. Aktories and A. Wegner, ADP-ribosylation of actin by clostridial toxins, The Journal of Cell Biology, vol.109, issue.4, pp.1385-1387, 1989.
DOI : 10.1083/jcb.109.4.1385

URL : http://europepmc.org/articles/pmc2115792?pdf=render

C. Weigt, I. Just, A. Wegner, and K. Aktories, Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments, FEBS Letters, vol.225, issue.1-2, pp.181-184, 1989.
DOI : 10.1016/0014-5793(87)81129-8

URL : http://onlinelibrary.wiley.com/doi/10.1016/0014-5793(89)80279-0/pdf

M. Miyake and I. Ohishi, Response of tissue-cultured cynomolgus monkey kidney cells to botulinum C2 toxin, Microbial Pathogenesis, vol.3, issue.4, pp.279-286, 1987.
DOI : 10.1016/0882-4010(87)90061-1

K. Heine, S. Pust, S. Enzenmüller, and H. Barth, ADP-Ribosylation of Actin by the Clostridium botulinum C2 Toxin in Mammalian Cells Results in Delayed Caspase-Dependent Apoptotic Cell Death, Infection and Immunity, vol.76, issue.10, pp.4600-4608, 2008.
DOI : 10.1128/IAI.00651-08

H. Hilger, S. Pust, V. Figura, G. Kaiser, E. Stiles et al., The Long-Lived Nature of Clostridium perfringens Iota Toxin in Mammalian Cells Induces Delayed Apoptosis, Infection and Immunity, vol.77, issue.12, pp.5593-5601, 2009.
DOI : 10.1128/IAI.00710-09

URL : http://iai.asm.org/content/77/12/5593.full.pdf

H. Barth and K. Aktories, New insights into the mode of action of the actin ADP-ribosylating virulence factors Salmonella enterica SpvB and Clostridium botulinum C2 toxin, European Journal of Cell Biology, vol.90, issue.11, 2011.
DOI : 10.1016/j.ejcb.2010.11.007

N. Fujii, T. Kubota, S. Shirakawa, K. Kimura, and I. Ohishi, Characterization of Component-I Gene of Botulinum C2 Toxin and PCR Detection of Its Gene in Clostridial Species, Biochemical and Biophysical Research Communications, vol.220, issue.2, pp.353-359, 1996.
DOI : 10.1006/bbrc.1996.0409

H. Barth, J. Preiss, F. Hofmann, and K. Aktories, C2 Toxin by Site-directed Mutagenesis, Journal of Biological Chemistry, vol.269, issue.45, pp.29506-29511, 1998.
DOI : 10.1073/pnas.85.20.7521

H. Barth, D. Blocker, J. Behlke, W. Bergsma-schutter, and A. Brisson, C2 Toxin Requires Oligomerization and Acidification, Journal of Biological Chemistry, vol.266, issue.25, pp.18704-18711, 2000.
DOI : 10.1038/385833a0

URL : http://www.jbc.org/content/275/25/18704.full.pdf

C. Sterthoff, A. Lang, C. Schwan, A. Tauch, and K. Aktories, Functional Characterization of an Extended Binding Component of the Actin-ADP-Ribosylating C2 Toxin Detected in Clostridium botulinum Strain (C) 2300, Infection and Immunity, vol.78, issue.4, pp.1468-1474, 2010.
DOI : 10.1128/IAI.01351-09

D. Blöcker, H. Barth, E. Maier, R. Benz, and J. Barbieri, The C Terminus of Component C2II of Clostridium botulinum C2 Toxin Is Essential for Receptor Binding, Infection and Immunity, vol.68, issue.8, pp.4566-4573, 2000.
DOI : 10.1128/IAI.68.8.4566-4573.2000

M. Eckhardt, H. Barth, D. Blöcker, and K. Aktories, C2 Toxin to Asparagine-linked Complex and Hybrid Carbohydrates, Journal of Biological Chemistry, vol.266, issue.4, pp.2328-2334, 2000.
DOI : 10.1146/annurev.ge.18.120184.002521

URL : http://www.jbc.org/content/275/4/2328.full.pdf

B. Stiles, D. Blöcker, M. Hale, M. Guetthoff, and H. Barth, Clostridium botulinum C2 toxin: binding studies with fluorescence-activated cytometry, Toxicon, vol.40, issue.8, pp.1135-1140, 2002.
DOI : 10.1016/S0041-0101(02)00113-7

C. Schleberger, H. Hochmann, H. Barth, K. Aktories, and G. Schulz, Structure and Action of the Binary C2 Toxin from Clostridium botulinum, Journal of Molecular Biology, vol.364, issue.4, pp.705-715, 2006.
DOI : 10.1016/j.jmb.2006.09.002

M. Nagahama, T. Hagiyama, T. Kojima, K. Aoyanagi, and C. Takahashi, Binding and Internalization of Clostridium botulinum C2 Toxin, Infection and Immunity, vol.77, issue.11, pp.5139-5148, 2009.
DOI : 10.1128/IAI.00638-09

URL : http://iai.asm.org/content/77/11/5139.full.pdf

S. Pust, H. Barth, and K. Sandvig, Clostridium botulinum C2 toxin is internalized by clathrin- and Rho-dependent mechanisms, Cellular Microbiology, vol.76, issue.12, pp.1809-1820, 2010.
DOI : 10.1091/mbc.10.8.2687

URL : http://onlinelibrary.wiley.com/doi/10.1111/j.1462-5822.2010.01512.x/pdf

G. Haug, J. Leemhuis, D. Tiemann, D. Meyer, and K. Aktories, C2 Toxin into the Cytosol, Journal of Biological Chemistry, vol.269, issue.34, pp.32266-32274, 2003.
DOI : 10.1083/jcb.200210028

E. Kaiser, S. Pust, C. Kroll, and H. Barth, C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells, Cellular Microbiology, vol.54, issue.5, pp.780-795, 2009.
DOI : 10.1111/j.1365-2958.1997.tb02669.x

A. Schmid, R. Benz, I. Just, and K. Aktories, Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes. Formation of cation-selective channels and inhibition of channel function by chloroquine, J Biol Chem, vol.269, pp.16706-16711, 1994.

C. Bachmeyer, R. Benz, H. Barth, K. Aktories, and M. Gilbert, C2 toxin with lipid bilayer membranes and Vero cells: inhibition of channel function by chloroquine and related compounds in vitro and intoxification in vivo, The FASEB Journal, vol.15, issue.9, pp.1658-1660, 2001.
DOI : 10.1096/fj.00-0671fje

D. Blöcker, K. Pohlmann, G. Haug, C. Bachmeyer, and R. Benz, C2 Toxin, Journal of Biological Chemistry, vol.10, issue.39, pp.37360-37367, 2003.
DOI : 10.1074/jbc.M303980200

D. Blöcker, J. Behlke, K. Aktories, and H. Barth, Cellular Uptake of the Clostridium perfringens Binary Iota-Toxin, Infection and Immunity, vol.69, issue.5, pp.2980-2987, 2001.
DOI : 10.1128/IAI.69.5.2980-2987.2001

O. Knapp, R. Benz, M. Gibert, J. Marvaud, and M. Popoff, Iota-Toxin with Lipid Bilayer Membranes, Journal of Biological Chemistry, vol.7, issue.8, pp.6143-6152, 2002.
DOI : 10.1038/385833a0

V. Karginov, E. Nestorovich, M. Moayeri, S. Leppla, and S. Bezrukov, Blocking anthrax lethal toxin at the protective antigen channel by using structure-inspired drug design, Proceedings of the National Academy of Sciences, vol.52, issue.22, pp.15075-15080, 2005.
DOI : 10.1074/jbc.M401980200

URL : http://www.pnas.org/content/102/42/15075.full.pdf

V. Karginov, E. Nestorovich, A. Yohannes, T. Robinson, and N. Fahmi, Search for Cyclodextrin-Based Inhibitors of Anthrax Toxins: Synthesis, Structural Features, and Relative Activities, Antimicrobial Agents and Chemotherapy, vol.50, issue.11, pp.3740-3753, 2006.
DOI : 10.1128/AAC.00693-06

URL : http://aac.asm.org/content/50/11/3740.full.pdf

V. Karginov, E. Nestorovich, F. Schmidtmann, T. Robinson, and A. Yohannes, Inhibition of S. aureus ??-hemolysin and B. anthracis lethal toxin by ??-cyclodextrin derivatives, Bioorganic & Medicinal Chemistry, vol.15, issue.16, pp.5424-5431, 2007.
DOI : 10.1016/j.bmc.2007.05.058

E. Nestorovich, V. Karginov, A. Berezhkovskii, and S. Bezrukov, Blockage of Anthrax PA63 Pore by a Multicharged High-Affinity Toxin Inhibitor, Biophysical Journal, vol.99, issue.1, pp.134-143, 2010.
DOI : 10.1016/j.bpj.2010.03.070

URL : https://doi.org/10.1016/j.bpj.2010.03.070

M. Moayeri, T. Robinson, S. Leppla, and V. Karginov, In Vivo Efficacy of ??-Cyclodextrin Derivatives against Anthrax Lethal Toxin, Antimicrobial Agents and Chemotherapy, vol.52, issue.6, pp.2239-2241, 2008.
DOI : 10.1128/AAC.00009-08

URL : http://aac.asm.org/content/52/6/2239.full.pdf

B. Ragle and V. Karginov, Prevention and Treatment of Staphylococcus aureus Pneumonia with a ??-Cyclodextrin Derivative, Antimicrobial Agents and Chemotherapy, vol.54, issue.1, pp.298-304, 2010.
DOI : 10.1128/AAC.00973-09

URL : http://aac.asm.org/content/54/1/298.full.pdf

M. Hale, J. Marvaud, M. Popoff, and B. Stiles, Detergent-Resistant Membrane Microdomains Facilitate Ib Oligomer Formation and Biological Activity of Clostridium perfringens Iota-Toxin, Infection and Immunity, vol.72, issue.4, pp.2186-2193, 2004.
DOI : 10.1128/IAI.72.4.2186-2193.2004

URL : http://iai.asm.org/content/72/4/2186.full.pdf

K. Sandvig and S. Olsnes, Diphtheria toxin entry into cells is facilitated by low pH, The Journal of Cell Biology, vol.87, issue.3, pp.828-832, 1980.
DOI : 10.1083/jcb.87.3.828

URL : http://jcb.rupress.org/content/jcb/87/3/828.full.pdf

A. Kintzer, K. Thoren, H. Sterling, K. Dong, and G. Feld, The Protective Antigen Component of Anthrax Toxin Forms Functional Octameric Complexes, Journal of Molecular Biology, vol.392, issue.3, pp.614-629, 2009.
DOI : 10.1016/j.jmb.2009.07.037

URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2742380

R. Blaustein, T. Koehler, R. Collier, and A. Finkelstein, Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers., Proceedings of the National Academy of Sciences, vol.86, issue.7, pp.2209-2213, 1989.
DOI : 10.1073/pnas.86.7.2209

URL : http://www.pnas.org/content/86/7/2209.full.pdf

R. Blaustein and A. Finkelstein, Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Effects on macroscopic conductance, The Journal of General Physiology, vol.96, issue.5, pp.905-919, 1990.
DOI : 10.1085/jgp.96.5.905

R. Blaustein, E. Lea, and A. Finkelstein, Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Single-channel analysis, The Journal of General Physiology, vol.96, issue.5, pp.921-942, 1990.
DOI : 10.1085/jgp.96.5.921

URL : http://jgp.rupress.org/content/jgp/96/5/921.full.pdf

F. Orlik, B. Schiffler, and R. Benz, Anthrax Toxin Protective Antigen: Inhibition of Channel Function by Chloroquine and Related Compounds and Study of Binding Kinetics Using the Current Noise Analysis, Biophysical Journal, vol.88, issue.3, pp.1715-1724, 2005.
DOI : 10.1529/biophysj.104.050336

D. Anderson and R. Blaustein, Preventing Voltage-dependent Gating of Anthrax Toxin Channels Using Engineered Disulfides, The Journal of General Physiology, vol.22, issue.3, pp.351-360, 2008.
DOI : 10.1529/biophysj.104.050864

URL : http://jgp.rupress.org/content/jgp/132/3/351.full.pdf

A. Delcour, Structure and function of pore-forming beta-barrels from bacteria, J Mol Microbiol Biotechnol, vol.4, pp.1-10, 2002.

C. Bachmeyer, F. Orlik, H. Barth, K. Aktories, and R. Benz, Mechanism of C2-toxin Inhibition by Fluphenazine and Related Compounds: Investigation of their Binding Kinetics to the C2II-channel using the Current Noise Analysis, Journal of Molecular Biology, vol.333, issue.3, pp.527-540, 2003.
DOI : 10.1016/j.jmb.2003.08.044

M. Backer, V. Patel, B. Jehning, K. Claffey, and V. Karginov, Inhibition of Anthrax Protective Antigen Outside and Inside the Cell, Antimicrobial Agents and Chemotherapy, vol.51, issue.1, pp.245-251, 2007.
DOI : 10.1128/AAC.00983-06

URL : http://aac.asm.org/content/51/1/245.full.pdf

M. Gibert, J. Marvaud, Y. Pereira, M. Hale, and B. Stiles, Differential requirement for the translocation of clostridial binary toxins: Iota toxin requires a membrane potential gradient, FEBS Letters, vol.281, issue.7, pp.1287-1296, 2007.
DOI : 10.1074/jbc.M600477200

B. Stiles, M. Hale, J. Marvaud, and M. Popoff, Clostridium perfringens Iota Toxin: Binding Studies and Characterization of Cell Surface Receptor by Fluorescence-Activated Cytometry, Infection and Immunity, vol.68, issue.6, pp.3475-3484, 2000.
DOI : 10.1128/IAI.68.6.3475-3484.2000

URL : http://iai.asm.org/content/68/6/3475.full.pdf

R. Collier, Membrane translocation by anthrax toxin, Molecular Aspects of Medicine, vol.30, issue.6, pp.413-422, 2009.
DOI : 10.1016/j.mam.2009.06.003

URL : http://europepmc.org/articles/pmc2783560?pdf=render

K. Thoren and B. Krantz, The unfolding story of anthrax toxin translocation, Molecular Microbiology, vol.455, issue.3, p.21443527, 2011.
DOI : 10.1038/nature07335

URL : http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2011.07614.x/pdf

N. Duesbery, C. Webb, S. Leppla, V. Gordon, and K. Klimpel, Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor, Science, vol.280, issue.5364, pp.734-737, 1998.
DOI : 10.1126/science.280.5364.734

G. Vitale, R. Pellizzari, C. Recchi, G. Napolitani, and M. Mock, Anthrax Lethal Factor Cleaves the N-Terminus of MAPKKs and Induces Tyrosine/Threonine Phosphorylation of MAPKs in Cultured Macrophages, Biochemical and Biophysical Research Communications, vol.248, issue.3, pp.706-711, 1998.
DOI : 10.1006/bbrc.1998.9040

F. Tonello and C. Montecucco, The anthrax lethal factor and its MAPK kinase-specific metalloprotease activity, Molecular Aspects of Medicine, vol.30, issue.6, pp.431-438, 2009.
DOI : 10.1016/j.mam.2009.07.006

S. Leppla, Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells., Proceedings of the National Academy of Sciences, vol.79, issue.10, pp.3162-3166, 1982.
DOI : 10.1073/pnas.79.10.3162

URL : http://www.pnas.org/content/79/10/3162.full.pdf

S. Leppla, Bacillus anthracis calmodulin-dependent adenylate cyclase: chemical and enzymatic properties and interactions with eukaryotic cells, Adv Cyclic Nucleotide Protein Phosphorylation Res, vol.17, pp.189-198, 1984.

K. Halverson, R. Panchal, T. Nguyen, R. Gussio, and S. Little, Anthrax Biosensor, Protective Antigen Ion Channel Asymmetric Blockade, Journal of Biological Chemistry, vol.266, issue.40, pp.34056-34062, 2005.
DOI : 10.1038/n35101998

URL : http://www.jbc.org/content/280/40/34056.full.pdf

G. Feld, K. Thoren, A. Kintzer, H. Sterling, and I. Tang, Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers, Nature Structural & Molecular Biology, vol.276, issue.11, pp.1383-1390, 2010.
DOI : 10.1021/bi015860m

URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3133606

A. Kintzer, H. Sterling, I. Tang, A. Gader, and A. Miles, Role of the Protective Antigen Octamer in the Molecular Mechanism of Anthrax Lethal Toxin Stabilization in Plasma, Journal of Molecular Biology, vol.399, issue.5, pp.741-758, 2010.
DOI : 10.1016/j.jmb.2010.04.041

B. Krantz, R. Melnyk, S. Zhang, S. Juris, and D. Lacy, A Phenylalanine Clamp Catalyzes Protein Translocation Through the Anthrax Toxin Pore, Science, vol.309, issue.5735, pp.777-781, 2005.
DOI : 10.1126/science.1113380

URL : http://europepmc.org/articles/pmc1815389?pdf=render

T. Neumeyer, B. Schiffler, E. Maier, A. Lang, and K. Aktories, C2 Toxin, Journal of Biological Chemistry, vol.100, issue.7, pp.3904-3914, 2008.
DOI : 10.1021/bi051830y

A. Díaz-moscoso, A. Méndez-ardoy, F. Ortega-caballero, J. Benito, O. Mellet et al., Symmetry Complementarity-Guided Design of Anthrax Toxin Inhibitors Based on ??-Cyclodextrin: Synthesis and Relative Activities of Face-Selective Functionalized Polycationic Clusters, ChemMedChem, vol.61, issue.1, pp.181-192, 2011.
DOI : 10.1016/j.bmc.2005.07.054

W. Li, T. Claridge, Q. Li, M. Wormald, and B. Davis, Tuning the Cavity of Cyclodextrins: Altered Sugar Adaptors in Protein Pores, Journal of the American Chemical Society, vol.133, issue.6, p.21244029, 2011.
DOI : 10.1021/ja1100867

S. Perelle, M. Domenighini, and M. Popoff, Evidence that Arg-295, Glu-378, and Glu-380 are active-site residues of the ADP-ribosyltransferase activity of iota toxin, FEBS Letters, vol.29, issue.2-3, pp.191-194, 1996.
DOI : 10.1016/0041-0101(91)90076-4

URL : http://onlinelibrary.wiley.com/doi/10.1016/0014-5793(96)01035-6/pdf

U. Laemmli, Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, Nature, vol.244, issue.5259, pp.680-685, 1970.
DOI : 10.1101/SQB.1963.028.01.053

M. Montal and P. Mueller, Formation of Bimolecular Membranes from Lipid Monolayers and a Study of Their Electrical Properties, Proceedings of the National Academy of Sciences, vol.69, issue.12, pp.3561-3566, 1972.
DOI : 10.1073/pnas.69.12.3561

URL : http://www.pnas.org/content/69/12/3561.full.pdf

J. Kasianowicz and S. Bezrukov, Protonation dynamics of the alpha-toxin ion channel from spectral analysis of pH-dependent current fluctuations, Biophysical Journal, vol.69, issue.1, pp.94-105, 1995.
DOI : 10.1016/S0006-3495(95)79879-4

F. Sigworth and S. Sine, Data transformations for improved display and fitting of single-channel dwell time histograms, Biophysical Journal, vol.52, issue.6, pp.1047-1054, 1987.
DOI : 10.1016/S0006-3495(87)83298-8

URL : https://doi.org/10.1016/s0006-3495(87)83298-8