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

S. Perelle, M. Gibert, P. Bourlioux, G. Corthier, M. R. Popoff et al., Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196 Clostridium difficile binary toxin CDT: Mechanism, epidemiology, and potential clinical importance Production of actin-specific ADP-ribosyltransferase (binary toxin) by strains of Clostridium difficile, Infect. Immun. Gut Microbes J.; Duerden, B FEMS Microbiol. Lett, vol.65, issue.186, pp.1402-1407, 1997.

J. G. Songer, B. G. Wilkins, T. D. Wilkins, and T. D. , Clostridial enteric diseases of domestic animals Purification and characterization of Clostridium perfringens iota toxin: Dependence on two nonlinked proteins for biological activity Clostridium perfringens iota toxin: Synergism between two proteins, Clin. Microbiol. Rev. Infect. Immun. Toxicon Off. J. Int. Soc.Toxinol, vol.9, issue.24, pp.216-234, 1986.

J. Sakurai, M. Nagahama, M. Oda, H. Tsuge, and K. Kobayashi, Clostridium perfringens Iota-Toxin: Structure and Function, Toxins, vol.581, issue.2, pp.208-228, 2009.
DOI : 10.1016/j.febslet.2007.02.041
URL : http://www.mdpi.com/2072-6651/1/2/208/pdf

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

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 and S. Tsuyama, ADP-ribosylation of nonmuscle actin with component I of C2 toxin, Biochemical and Biophysical Research Communications, vol.136, issue.2, pp.802-806, 1986.
DOI : 10.1016/0006-291X(86)90511-5

H. Barth, K. Aktories, M. R. Popoff, and B. G. 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

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, pp.944-950, 2011.
DOI : 10.1016/j.ejcb.2010.11.007

H. Barth, D. Blöcker, J. Behlke, W. Bergsma-schutter, A. Brisson et al., 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

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

B. G. Stiles, M. L. Hale, J. C. Marvaud, and M. R. 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

B. G. Stiles, M. L. Hale, J. C. Marvaud, and M. R. Popoff, Clostridium perfringens iota toxin: characterization of the cell-associated iota b complex, Biochemical Journal, vol.367, issue.3, pp.801-808, 2002.
DOI : 10.1042/bj20020566

P. Papatheodorou, J. E. Carette, G. W. Bell, C. Schwan, G. Guttenberg et al., Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT), Proc. Natl. Acad. Sci. USA 2011, pp.16422-16427
DOI : 10.1128/IAI.69.5.2980-2987.2001
URL : http://www.pnas.org/content/108/39/16422.full.pdf

P. Papatheodorou, C. Wilczek, T. Nölke, G. Guttenberg, D. Hornuss et al., ABSTRACT, Infection and Immunity, vol.80, issue.4, pp.1418-1423, 2012.
DOI : 10.1128/IAI.06378-11

P. Papatheodorou, D. Hornuss, T. Nölke, S. Hemmasi, J. Castonguay et al., Clostridium difficile Binary Toxin CDT Induces Clustering of the Lipolysis-Stimulated Lipoprotein Receptor into Lipid Rafts, mBio, vol.4, issue.3
DOI : 10.1128/mBio.00244-13
URL : http://mbio.asm.org/content/4/3/e00244-13.full.pdf

D. J. Wigelsworth, G. Ruthel, L. Schnell, P. Herrlich, J. Blonder et al., CD44 Promotes Intoxication by the Clostridial Iota-Family Toxins, PLoS ONE, vol.163, issue.12, p.51356, 2012.
DOI : 10.1371/journal.pone.0051356.g004
URL : https://hal.archives-ouvertes.fr/pasteur-01764029

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

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

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, M. Gilbert et al., 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

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

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

M. Gibert, J. C. Marvaud, Y. Pereira, M. L. Hale, B. G. Stiles et al., 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

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

G. Haug, K. Aktories, and H. Barth, The Host Cell Chaperone Hsp90 Is Necessary for Cytotoxic Action of the Binary Iota-Like Toxins, Infection and Immunity, vol.72, issue.5, pp.3066-3068, 2004.
DOI : 10.1128/IAI.72.5.3066-3068.2004

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

E. Kaiser, C. Kroll, K. Ernst, C. Schwan, M. R. Popoff et al., ABSTRACT, Infection and Immunity, vol.79, issue.10, pp.3913-3921, 2011.
DOI : 10.1128/IAI.05372-11

E. Kaiser, N. Böhm, K. Ernst, S. Langer, C. Schwan et al., FK506-binding protein 51 interacts with Clostridium botulinum C2 toxin and FK506 blocks membrane translocation of the toxin in mammalian cells, Cell. Microbiol, vol.4, pp.1193-1205, 2012.

K. Ernst, S. Langer, E. Kaiser, C. Osseforth, J. Michaelis et al., Cyclophilin-Facilitated Membrane Translocation as Pharmacological Target to Prevent Intoxication of Mammalian Cells by Binary Clostridial Actin ADP-Ribosylated Toxins, Journal of Molecular Biology, vol.427, issue.6, pp.1224-1238, 2015.
DOI : 10.1016/j.jmb.2014.07.013
URL : https://hal.archives-ouvertes.fr/pasteur-01768428

I. Gülke, G. Pfeifer, J. Liese, M. Fritz, F. Hofmann et al., 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

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

J. Vandekerckhove, B. Schering, M. Bärmann, 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

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

B. Schering, M. Bärmann, G. S. Chhatwal, U. Geipel, and K. Aktories, ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin, European Journal of Biochemistry, vol.247, issue.1-2, pp.225-229, 1988.
DOI : 10.1042/bj2470363

H. Barth, J. C. 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

S. Perelle, M. Domenighini, and M. R. 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.2-3, 1996.
DOI : 10.1016/0041-0101(91)90076-4

H. Tsuge, M. Nagahama, M. Oda, S. Iwamoto, H. Utsunomiya et al., Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens iota-toxin, Proc. Natl. Acad. Sci, pp.7399-7404, 2008.
DOI : 10.1073/pnas.0801215105
URL : http://www.pnas.org/content/105/21/7399.full.pdf

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

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

W. Wiegers, I. Just, H. Müller, A. Hellwig, P. Traub et al., 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.

C. Schwan, B. Stecher, T. Tzivelekidis, M. Van-ham, M. Rohde et al., Clostridium difficile Toxin CDT Induces Formation of Microtubule-Based Protrusions and Increases Adherence of Bacteria, PLoS Pathogens, vol.23, issue.12, p.1000626, 2009.
DOI : 10.1371/journal.ppat.1000626.s010
URL : https://doi.org/10.1371/journal.ppat.1000626

K. Aktories, Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence, Proc. Natl. Acad. Sci. USA 2014, pp.2313-2318

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, G. Von-figura, B. G. Stiles, M. R. Popoff 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

L. Heinlen and J. Ballard, Clostridium difficile Infection, The American Journal of the Medical Sciences, vol.340, issue.3, pp.247-252, 2010.
DOI : 10.1097/MAJ.0b013e3181e939d8

I. Just, J. Selzer, M. Wilm, C. Von-eichel-streiber, M. Mann et al., Glucosylation of Rho proteins by Clostridium difficile toxin B, Nature, vol.375, issue.6531, pp.500-503, 1995.
DOI : 10.1038/375500a0

I. Just, M. Wilm, J. Selzer, G. Rex, C. Von-eichel-streiber et al., (ToxA) Monoglucosylates the Rho Proteins, Journal of Biological Chemistry, vol.8, issue.23, pp.13932-13936, 1995.
DOI : 10.1002/bms.1200111109
URL : http://www.jbc.org/content/270/23/13932.full.pdf

T. Jank and K. Aktories, Structure and mode of action of clostridial glucosylating toxins: the ABCD model, Trends in Microbiology, vol.16, issue.5, pp.222-229, 2008.
DOI : 10.1016/j.tim.2008.01.011

B. Geric, M. Rupnik, D. N. Gerding, M. Grabnar, and S. Johnson, Distribution of Clostridium difficile variant toxinotypes and strains with binary toxin genes among clinical isolates in an American hospital, Journal of Medical Microbiology, vol.53, issue.9, pp.887-894, 2004.
DOI : 10.1099/jmm.0.45610-0
URL : http://jmm.microbiologyresearch.org/deliver/fulltext/jmm/53/9/JMM5309.887.pdf?itemId=/content/journal/jmm/10.1099/jmm.0.45610-0&mimeType=pdf&isFastTrackArticle=

C. Goncalves, D. Decre, F. Barbut, B. Burghoffer, and J. C. Petit, Prevalence and Characterization of a Binary Toxin (Actin-Specific ADP-Ribosyltransferase) from Clostridium difficile, Journal of Clinical Microbiology, vol.42, issue.5, pp.1933-1939, 2004.
DOI : 10.1128/JCM.42.5.1933-1939.2004
URL : http://jcm.asm.org/content/42/5/1933.full.pdf

H. Martin, B. Willey, D. E. Low, H. R. Staempfli, A. Mcgeer et al., Characterization of Clostridium difficile Strains Isolated from Patients in Ontario, Canada, from 2004 to 2006, Journal of Clinical Microbiology, vol.46, issue.9, pp.2999-3004, 2004.
DOI : 10.1128/JCM.02437-07
URL : http://jcm.asm.org/content/46/9/2999.full.pdf

S. A. Kuehne, M. M. Collery, M. L. Kelly, S. T. Cartman, A. Cockayne et al., Importance of Toxin A, Toxin B, and CDT in Virulence of an Epidemic Clostridium difficile Strain, The Journal of Infectious Diseases, vol.40, issue.1, pp.83-86, 2014.
DOI : 10.1086/427113

J. A. Young and R. J. Collier, Anthrax Toxin: Receptor Binding, Internalization, Pore Formation, and Translocation, Annual Review of Biochemistry, vol.76, issue.1, pp.243-265, 2007.
DOI : 10.1146/annurev.biochem.75.103004.142728

E. J. Gillespie, C. L. Ho, K. Balaji, D. L. Clemens, G. Deng et al., Selective inhibitor of endosomal trafficking pathways exploited by multiple toxins and viruses, Proc. Natl. Acad. Sci. USA 2013, pp.4904-4912
DOI : 10.1016/0092-8674(84)90070-9
URL : http://www.pnas.org/content/110/50/E4904.full.pdf

U. K. 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