V. I. Roxas-duncan and L. A. Smith, Bacterial protein toxins as biological weapons, The Comprehensive Sourcebook of Bacterial Protein Toxins, pp.1135-1149, 2015.

J. Jankovic, Botulinum toxin: State of the art, Movement Disorders, vol.32, issue.8, pp.1131-1138, 2017.

J. Jankovic, An update on new and unique uses of botulinum toxin in movement disorders, Toxicon, vol.147, pp.84-88, 2018.

J. K. Torrens, Clostridium botulinum was named because of association with "sausage poisoning", BMJ, vol.316, issue.7125, p.151, 1998.

M. R. Popoff and C. Mazuet, In: Clostridium botulinum, A Spore Forming Organism and a Challenge to Food Safety, NovaAdvances in Food Safety and Food Micorbiology, pp.1-36, 2012.

P. Emsley, C. Fotinou, I. Black, N. F. Fairweather, I. G. Charles et al., The structures of the Hc fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding, The Journal of Biological Chemistry, vol.275, issue.12, pp.8889-8894, 2000.

D. B. Lacy and R. C. Stevens, Sequence homology and structural analysis of the clostridial neurotoxins, Journal of Molecular Biology, vol.291, issue.5, pp.1091-1104, 1999.

D. B. Lacy, W. Tepp, A. C. Cohen, D. Gupta, B. R. Stevens et al., Crystal structure of botulinum neurotoxin type A and implications for toxicity, Nature Structural Biology, vol.5, issue.10, pp.898-902, 1998.

T. C. Umland, L. M. Wingert, S. Swaminathan, W. F. Furey, J. J. Schmidt et al., The structure of the receptor binding fragment H c of tetanus neurotoxin, Nature Structural Biology, vol.4, issue.10, pp.788-792, 1997.

C. Fotinou, P. Emsley, I. Black, H. Ando, H. Ishida et al., The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin, The Journal of Biological Chemistry, vol.276, issue.34, pp.3274-3281, 2001.

M. A. Breidenbach and A. T. Brunger, 2.3 A crystal structure of tetanus neurotoxin light chain, Biochemistry, vol.44, issue.20, pp.7450-7457, 2005.
URL : https://hal.archives-ouvertes.fr/in2p3-00019515

Z. Fu, S. Chen, M. R. Baldwin, G. E. Boldt, A. Crawford et al., Light chain of botulinum neurotoxin serotype A: structural resolution of a catalytic intermediate, Biochemistry, vol.45, issue.29, pp.8903-8911, 2006.

S. Swaminathan and S. Eswaramoorthy, Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B, Nature Structural Biology, vol.7, issue.8, pp.693-699, 2000.

P. Stenmark, J. Dupuy, A. Imamura, M. Kiso, and R. C. Stevens, Crystal structure of botulinum neurotoxin type A in complex with the cell surface co-receptor GT1b-insight into the toxin-neuron interaction, PLoS Pathogens, vol.4, issue.8, p.1000129, 2008.

D. Kumaran, S. Eswaramoorthy, W. Furey, J. Navaza, M. Sax et al., Domain organization in Clostridium botulinum neurotoxin type E is unique: Its implication in faster translocation, Journal of Molecular Biology, vol.386, issue.1, pp.233-245, 2009.

S. Swaminathan, Molecular structures and functional relationships in clostridial neurotoxins, The FEBS Journal, vol.278, issue.23, pp.4467-4485, 2011.

M. R. Popoff and J. C. Marvaud, Structural and genomic features of clostridial neurotoxins, The Comprehensive Sourcebook of Bacterial Protein Toxins. 2, pp.174-201, 1999.

B. Poulain, M. R. Popoff, and J. Molgo, How do the botulinum neurotoxins block neurotransmitter release: From botulism to the molecular mechanism of action, Botulinum Journal, vol.1, issue.1, pp.14-87, 2008.
URL : https://hal.archives-ouvertes.fr/hal-00303601

M. W. Peck, T. J. Smith, F. Anniballi, J. W. Austin, L. Bano et al., Historical perspectives and guidelines for Botulinum neurotoxin subtype nomenclature, Toxins (Basel), vol.9, issue.1, p.38, 2017.
URL : https://hal.archives-ouvertes.fr/pasteur-01821691

B. R. Singh, T. Wang, R. Kukreja, and S. Cai, The botulinum neurotoxin complex and the role of ancillary proteins, Molecular Aspects of Botulinum Neurotoxin. Current Topics in Neurotoxicity, vol.4, pp.68-101, 2014.

S. K. Sharma, M. A. Ramzan, and B. R. Singh, Separation of the components of type A botulinum neeurotoxin complex by electrophoresis, Toxicon, vol.41, issue.3, pp.321-331, 2003.

K. Oguma, K. Inoue, Y. Fujinaga, K. Yokota, T. Watanabe et al., Structure and function of Clostridium botulinum progenitor toxin, Journal of Toxicology, vol.18, pp.17-34, 1999.

S. Gu and J. R. , Assembly and function of the botulinum neurotoxin progenitor complex, Current Topics in Microbiology and Immunology, vol.364, 2013.

K. Lee, S. Gu, J. L. Le, T. T. Cheng, L. W. Strotmeier et al., Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity, PLoS Pathogens, vol.9, issue.10, 2013.

D. A. Benefield, S. K. Dessain, N. Shine, M. D. Ohi, and D. B. Lacy, Molecular assembly of botulinum neurotoxin progenitor complexes, Proceedings of the National Academy of Sciences of the United States of America, vol.110, issue.14, pp.5630-5635, 2013.

S. Gu, S. Rumpel, J. Zhou, J. Strotmeier, H. Bigalke et al., Botulinum neurotoxin is shielded by NTNHA in an interlocked complex, Science, vol.335, issue.6071, pp.977-981, 2012.

A. M. Bryant, J. Davis, S. Cai, and B. R. Singh, Molecular composition and extinction coefficient of native botulinum neurotoxin complex produced by Clostridium botulinum hall A strain, The Protein Journal, vol.32, issue.2, pp.106-117, 2013.

K. Inoue, Y. Fujinaga, T. Watanabe, T. Ohyama, K. Takeshi et al., Molecular composition of Clostridium botulinum type A progenitor toxins, Infection and Immunity, vol.64, issue.5, pp.1589-1594, 1996.

M. A. Lietzow, E. T. Gielow, D. Le, J. Zhang, and M. F. Verhagen, Subunit stoichiometry of the Clostridium botulinum type A neurotoxin complex determined using denaturing capillary electrophoresis, The Protein Journal, vol.27, issue.7-8, pp.420-425, 2008.

S. S. Dineen, M. Bradshaw, and E. A. Johnson, Neurotoxin gene clusters in Clostridium botulinum type A strains: Sequence comparison and evolutionary implications, Current Microbiology, vol.46, issue.5, pp.342-352, 2003.

G. Lin, W. H. Tepp, C. L. Pier, M. J. Jacobson, and E. A. Johnson, Expression of the Clostridium botulinum A2 neurotoxin gene cluster proteins and characterization of the A2 complex, Applied and Environmental Microbiology, vol.76, issue.1, pp.40-47, 2010.

H. B. Hines, F. Lebeda, M. Hale, and E. E. Brueggemann, Characterization of botulinum progenitor toxins by mass spectrometry, Applied and Environmental Microbiology, vol.71, issue.8, pp.4478-4486, 2005.

B. Li, X. Qian, H. K. Sarkar, and B. R. Singh, Molecular characterization of type E Clostridium botulinum and comparison to other types of Clostridium botulinum, Biochimica et Biophysica Acta, vol.1395, pp.21-27, 1998.

R. Gustafsson, R. P. Berntsson, M. Martinez-carranza, E. Tekle, G. Odegrip et al., Crystal structures of OrfX2 and P47 from a Botulinum neurotoxin OrfX-type gene cluster, FEBS Letters, vol.591, issue.22, pp.3781-3792, 2017.

R. Fujita, Y. Fujinaga, K. Inoue, H. Nakajima, H. Kumon et al., Molecular characterization of two forms of nontoxic-non hemagglutinantinin components of Clostridium botulinum type A progenitor toxins, FEBS Letters, vol.376, pp.41-44, 1995.

Y. Sagane, T. Watanabe, H. Kouguchi, H. Sunagawa, K. Inoue et al., Characterization of nicking of the nontoxic-nonhemagglutinin components of Clostridium botulinum types C and D progenitor toxin, Journal of Protein Chemistry, vol.19, pp.575-581, 2000.

S. Eswaramoorthy, J. Sun, H. Li, B. R. Singh, and S. Swaminathan, Molecular assembly of Clostridium botulinum progenitor M complex of type E, Scientific Reports, vol.5, p.17795, 2015.

K. Inui, Y. Sagane, K. Miyata, S. Miyashita, T. Suzuki et al., Toxic and nontoxic components of botulinum neurotoxin complex are evolved from a common ancestral zinc protein, Biochemical and Biophysical Research Communications, vol.419, issue.3, pp.500-504, 2012.

K. Inoue, Y. Fujnaga, K. Honke, H. Arimitsu, N. Mahmut et al., Clostridium botulinum type A haemagglutinin positive progenitor toxin (HA + -PTX) binds to oligosaccharides containing Galb1-4GlcNAc through one subcomponent of haemagglutinin (HA1), Microbiology, vol.147, pp.811-819, 2001.

K. Inoue, Y. Fujinaga, K. Honke, K. Yokota, T. Ikeda et al., Characterization of haemagglutinin activity of Clostridium botulinum type C and D 16S toxins, and one subcomponent of haemagglutinin (HA1), Microbiology, vol.145, pp.2533-2542, 1999.

Y. Fujinaga, K. Inoue, S. Watarai, G. Sakaguchi, H. Arimitsu et al., Molecular characterization of binding subcomponents of Clostridium botulinum type C progenitor toxin for intestinal epithelial cells and erythrocytes, Microbiology, vol.150, issue.5, pp.1529-1538, 2004.

N. Mahmut, K. Inoue, Y. Fujinaga, L. Hughes, H. Arimitsu et al., Characteriza tion of monoclonal antibodies against haemagglutinin associated with Clostridium botulinum type C neurotoxin, Journal of Medical Microbiology, vol.51, pp.286-294, 2002.

S. K. Sharma, F. N. Fu, and B. R. Singh, Molecular properties of a hemagglutinin purified from type A Clostridium botulinum, Journal of Protein Chemistry, vol.18, pp.29-38, 1999.

Y. Sagane, H. Kouguchi, T. Watanabe, H. Sunagawa, K. Inoue et al., Role of C-terminal region, of HA-33 component of botulinum toxin in hemagglutination, Biochem ical and Biophysical Research Communications, vol.288, pp.650-657, 2001.

J. W. Arndt, J. Gu, L. Jaroszewski, R. Schwarzenbacher, M. A. Hanson et al., The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring beta-trefoil fold in the progenitor toxin complex, Journal of Molecular Biology, vol.346, issue.4, pp.1083-1093, 2005.

K. Inoue, M. Sobhany, T. R. Transue, K. Oguma, L. C. Pedersen et al., Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum, Microbiology, vol.149, pp.3361-3370, 2003.

K. Lee, K. H. Lam, A. M. Kruel, K. Perry, A. Rummel et al., High-resolution crystal structure of HA33 of botulinum neurotoxin type B progenitor toxin complex, Biochemical and Biophysical Research Communications, vol.446, issue.2, pp.568-573, 2014.

T. Nakamura, M. Kotani, T. Tonozuka, A. Ide, K. Oguma et al., Crystal structure of the HA3 subcomponent of Clostridium botulinum type C progenitor toxin, Journal of Molecular Biology, vol.385, issue.4, pp.1193-1206, 2009.

K. Hasegawa, T. Watanabe, T. Suzuki, A. Yamano, T. Oikawa et al., A novel subunit structure of Clostridium botulinum serotype D toxin complex with three extended arms, The Journal of Biological Chemistry, vol.282, issue.34, pp.24777-24783, 2007.

Y. Sugawara, T. Matsumura, Y. Takegahara, Y. Jin, Y. Tsukasaki et al., Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cad herin, The Journal of Cell Biology, vol.189, issue.4, pp.691-700, 2010.

K. Lee, X. Zhong, S. Gu, A. M. Kruel, M. B. Dorner et al., Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex, Science, vol.344, issue.6190, pp.1405-1410, 2014.

Y. Sugawara, M. Yutani, S. Amatsu, T. Matsumura, and Y. Fujinaga, Functional dissection of the Clostridium botulinum type B Hemagglutinin complex: Identification of the carbohydrate and E-cadherin binding sites, PLoS One, vol.9, issue.10, 2014.

M. J. Jacobson, G. Lin, B. Raphael, J. Andreadis, and E. A. Johnson, Analysis of neurotoxin cluster genes in Clostridium botulinum strains producing botulinum neurotoxin serotype A subtypes, Applied and Environmental Microbiology, vol.74, issue.9, pp.2778-2786, 2008.

S. S. Dineen, M. Bradshaw, C. E. Karasek, and E. A. Johnson, Nucleotide sequence and transcriptional analysis of the type A2 neurotoxin gene cluster in Clostridium botulinum, FEMS Microbiology Letters, vol.235, pp.9-16, 2004.

K. K. Hill and T. J. Smith, Genetic diversity within Clostridium botulinum serotypes, botulinum neurotoxin gene clusters and toxin subtypes, Current Topics in Microbiology and Immunology, vol.364, pp.1-20, 2013.

N. Dover, J. R. Barash, K. K. Hill, K. W. Davenport, H. Teshima et al., Clostridium botulinum strain Af84 contains three neurotoxin gene clusters: Bont/A2, bont/F4 and bont/F5, PLoS One, vol.8, p.61205, 2013.

B. Poulain, B. G. Stiles, M. R. Popoff, and J. Molgó, Attack of the nervous system by clostridial toxins: Physical findings, cellular and molecular actions, Alouf JE, Popoff MR, editors. The Sourcebook of Bacterial Protein Toxins, pp.348-389, 2006.

K. K. Hill, G. Xie, B. T. Foley, T. J. Smith, A. C. Munk et al., Recombination and insertion events involving the botulinum neurotoxin complex genes in Clostridium botulinum types A, B, E and F and Clostridium butyricum type E strains, BMC Biology, vol.7, p.66, 2009.

A. T. Carter, J. W. Austin, K. A. Weedmark, C. Corbett, and M. W. Peck, Three classes of plasmid (47-63 kb) carry the type B neurotoxin gene cluster of group II Clostridium botulinum

, Genome Biology and Evolution, vol.6, issue.8, pp.2076-2087, 2014.

K. M. Marshall, M. Bradshaw, and E. A. Johnson, Conjugative Botulinum neurotoxin-encoding plasmids in Clostridium botulinum, PLoS One, vol.5, issue.6, p.11087, 2010.

, Mode of Action, Botulinum Toxins

T. J. Smith, K. K. Hill, and B. H. Raphael, Historical and current perspectives on Clostridium botulinum diversity, Research in Microbiology, vol.166, issue.4, pp.290-302, 2015.

H. Skarin and B. Segerman, Horizontal gene transfer of toxin genes in Clostridium botulinum: Involvement of mobile elements and plasmids, Mobile Genetic Elements, vol.1, issue.3, pp.213-215, 2011.

M. R. Popoff and P. Bouvet, Genetic characteristics of toxigenic Clostridia and toxin gene evolution, Toxicon, vol.75, pp.63-89, 2013.
URL : https://hal.archives-ouvertes.fr/pasteur-01793259

B. Poulain, J. Molgo, and M. R. Popoff, Clostridial neurotoxins: From the cellular and molecular mode of action to their therapeutic use, The Comprehensive Sourcebook of Bacterial Protein Toxins, pp.287-336, 2015.

T. J. Smith, K. K. Hill, B. T. Foley, J. C. Detter, A. C. Munk et al., Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids, PLoS One, vol.2, issue.12, p.1271, 2007.

T. J. Smith, K. K. Hill, G. Xie, B. T. Foley, C. H. Williamson et al., Genomic sequences of six botulinum neurotoxin-producing strains representing three clostridial species illustrate the mobility and diversity of botulinum neurotoxin genes, Infection, Genetics and Evolution, vol.30, pp.102-113, 2015.

J. R. Barash and S. S. Arnon, A novel strain of Clostridium botulinum that produces type B and type H Botulinum toxins, The Journal of Infectious Diseases, vol.209, issue.2, pp.183-191, 2013.

N. Dover, J. R. Barash, K. K. Hill, G. Xie, and S. S. Arnon, Molecular characterization of a novel botulinum neurotoxin type H gene, The Journal of Infectious Diseases, vol.209, issue.2, pp.192-202, 2013.

S. Zhang, G. Masuyer, J. Zhang, Y. Shen, D. Lundin et al., Identification and characterization of a novel botulinum neurotoxin, Nature Communications, vol.8, p.14130, 2017.

I. Zornetta, A. Tehran, D. Arrigoni, G. Anniballi, F. Bano et al., The first non Clostridial botulinum-like toxin cleaves VAMP within the juxtamembrane domain, Scientific Reports, vol.6, p.30257, 2016.

J. Brunt, A. T. Carter, S. C. Stringer, and M. W. Peck, Identification of a novel botulinum neurotoxin gene cluster in Enterococcus, FEBS Letters, vol.592, pp.310-317, 2018.

S. Zhang, F. Lebreton, M. J. Mansfield, S. I. Miyashita, J. Zhang et al., Identifi cation of a botulinum neurotoxin-like toxin in a commensal strain of Enterococcus faecium, Cell Host & Microbe, vol.23, issue.2, p.6, 2018.

T. Wentz, Closed genome of Chryseobacterium piperi and identification and analysis of neurotoxin-like gene clusters, 11th Annual Botulinum Research Symposium, 2017.

, Botulinum Toxin, vol.22

A. C. Doxey, M. D. Lynch, K. M. Muller, E. M. Meiering, and B. J. Mcconkey, Insights into the evolutionary origins of clostridial neurotoxins from analysis of the Clostridium botulinum strain A neurotoxin gene cluster, BMC Evolutionary Biology, vol.8, p.316, 2008.

A. C. Doxey, M. J. Mansfield, and C. Montecucco, Discovery of novel bacterial toxins by genomics and computational biology, Toxicon, vol.147, pp.2-12, 2018.

T. J. Smith, J. Lou, I. N. Geren, C. M. Forsyth, R. Tsai et al., Sequence variation within botulinum neurotoxin serotypes impacts antibody binding and neutralization, Infection and Immunity, vol.73, issue.9, pp.5450-5457, 2005.

C. L. Pier, C. Chen, W. H. Tepp, G. Lin, K. D. Janda et al., Botulinum neurotoxin subtype A2 enters neuronal cells faster than subtype A1, FEBS Letters, vol.585, pp.199-206, 2011.

A. R. Kroken, F. C. Blum, M. Zuverink, and J. T. Barbieri, Entry of Botulinum neurotoxin subtypes A1 and A2 into neurons, Infection and Immunity, vol.85, issue.1, pp.795-811, 2017.

S. Pellett, W. H. Tepp, R. C. Whitemarsh, M. Bradshaw, and E. A. Johnson, In vivo onset and duration of action varies for botulinum neurotoxin A subtypes 1-5, Toxicon, vol.107, pp.37-42, 2015.

Y. Torii, Y. Goto, S. Nakahira, S. Kozaki, and A. Ginnaga, Comparison of the immunogenicity of botulinum toxin type A and the efficacy of A1 and A2 neurotoxins in animals with A1 toxin antibodies, Toxicon, vol.77, pp.114-120, 2014.

R. Kaji, Clinical differences between A1 and A2 botulinum toxin subtypes, Toxicon, vol.107, pp.85-88, 2015.

Y. Torii, Y. Goto, S. Nakahira, S. Kozaki, R. Kaji et al., Comparison of systemic toxicity between Botulinum toxin subtypes A1 and A2 in mice and rats, Basic & Clinical Pharmacology & Toxicology, vol.116, issue.6, pp.524-528, 2015.

M. Itakura, T. Kohda, T. Kubo, Y. Semi, Y. T. Azuma et al., Botulinum neurotoxin A subtype 2 reduces pathological behaviors more effectively than subtype 1 in a rat Parkinson's disease model, Biochemical and Biophysical Research Communications, vol.447, issue.2, pp.311-314, 2014.

S. Kull, K. M. Schulz, J. Weisemann, S. Kirchner, T. Schreiber et al., Isolation and functional characterization of the novel Clostridium botulinum neurotoxin A8 subtype, PLoS One, vol.10, issue.2, p.116381, 2015.

S. Kozaki, Y. Kamata, T. Nishiki, H. Kakinuma, H. Maruyama et al., Character ization of Clostridium botulinum type B neurotoxin associated with infant botulism in Japan, Infection and Immunity, vol.66, issue.10, pp.4811-4816, 1998.

S. R. Kalb, J. Baudys, R. P. Webb, P. Wright, T. J. Smith et al., Discovery of a novel enzymatic cleavage site for botulinum neurotoxin F5, FEBS Letters, vol.586, issue.2, pp.109-115, 2012.

S. R. Kalb, W. I. Santana, I. N. Geren, C. Garcia-rodriguez, J. Lou et al., Extraction and inhibition of enzymatic activity of botulinum neurotoxins /B1, /B2, /B3, /B4, and /B5 by a panel of monoclonal anti-BoNT/B antibodies, BMC Biochemistry, vol.12, p.58, 2011.

C. Mazuet, J. Dano, M. R. Popoff, C. Creminon, and H. Volland, Characterization of botulinum neurotoxin type A neutralizing monoclonal antibodies and influence of their half-lives on therapeutic activity, PLoS One, vol.5, issue.8, p.12416, 2010.
URL : https://hal.archives-ouvertes.fr/pasteur-01762095

S. R. Kalb, J. Lou, C. Garcia-rodriguez, I. N. Geren, T. J. Smith et al., Extraction and inhibition of enzymatic activity of botulinum neurotoxins/A1, /A2, and /A3 by a panel of monoclonal anti-BoNT/A antibodies, PLoS One, vol.4, issue.4, p.5355, 2009.

C. Connan and M. R. Popoff, Uptake of Clostridial neurotoxins into cells and dissemination. Current Topics in Microbiology and Immunology, vol.406, pp.39-78, 2017.
URL : https://hal.archives-ouvertes.fr/pasteur-01826649

Y. Fujinaga and M. R. Popoff, Translocation and dissemination of botulinum neurotoxin from the intestinal tract, Toxicon, vol.147, pp.13-18, 2018.
URL : https://hal.archives-ouvertes.fr/pasteur-01826790

M. Dong, H. Liu, W. H. Tepp, E. A. Johnson, R. Janz et al., Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons, Molecular Biology of the Cell, vol.19, issue.12, pp.5226-5237, 2008.

M. Dong, W. H. Tepp, H. Liu, E. A. Johnson, and E. R. Chapman, Mechanism of botulinum neurotoxin B and G entry into hippocampal neurons, The Journal of Cell Biology, 2007.

M. Dong, F. Yeh, W. H. Tepp, C. Dean, E. A. Johnson et al., SV2 is the protein receptor for Botulinum neurotoxin A, Science, vol.312, pp.592-596, 2006.

S. Mahrhold, A. Rummel, H. Bigalke, B. Davletov, and T. Binz, The synaptic vesicle protein 2C mediates the uptake of botulinum neurotoxin A into phrenic nerves, FEBS Letters, vol.580, pp.2011-2014, 2006.

T. Nishiki, Y. Kamata, Y. Nemoto, A. Omori, T. Ito et al., Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes, The Journal of Biological Chemistry, vol.269, issue.14, pp.10498-10503, 1994.

A. Rummel, K. Hafner, S. Mahrhold, N. Darashchonak, M. Holt et al., Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor, Journal of Neurochemistry, vol.110, issue.6, pp.1942-1954, 2009.

A. Rummel, T. Karnath, T. Henke, H. Bigalke, and T. Binz, Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G, The Journal of Biological Chemistry, vol.279, pp.30865-30870, 2004.

K. Tsukamoto, Y. Kozai, H. Ihara, T. Kohda, M. Mukamoto et al., Identification of the receptor-binding sites in the carboxyl-terminal half of the heavy chain of botulinum neurotoxin types C and D. Microbial Pathogenesis, vol.44, pp.484-493, 2008.

L. Peng, W. H. Tepp, E. A. Johnson, and M. Dong, Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors, PLoS Pathogens, vol.7, issue.3, p.1002008, 2011.

A. R. Kroken, A. P. Karalewitz, Z. Fu, J. J. Kim, and J. T. Barbieri, Novel ganglioside-mediated entry of botulinum neurotoxin serotype D into neurons, The Journal of Biological Chemistry, vol.286, pp.26828-26837, 2011.

L. Muraro, S. Tosatto, L. Motterlini, O. Rossetto, and C. Montecucco, The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane, Biochemical and Biophysical Research Communications, vol.380, issue.1, pp.76-80, 2009.

M. Galloux, H. Vitrac, C. Montagner, S. Raffestin, M. R. Popoff et al., Membrane interaction of botulinum neurotoxin A translocation (T) domain. The belt region is a regulatory loop for membrane interaction, Journal of Biological Chemistry, vol.283, issue.41, pp.27668-27676, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01187636

L. K. Koriazova and M. Montal, Translocation of botulinum neurotoxin light chain protease through the heavy chain channel, Nature Structural Biology, vol.10, issue.1, pp.13-18, 2003.

A. Fischer and M. Montal, Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes, The Journal of Biological Chemistry, vol.282, issue.40, pp.29604-29611, 2007.

A. Fischer, D. J. Mushrush, D. B. Lacy, and M. Montal, Botulinum neurotoxin devoid of receptor binding domain translocates active protease, PLoS Pathogens, vol.4, issue.12, p.1000245, 2008.

Y. Humeau, F. Doussau, N. J. Grant, and B. Poulain, How botulinum and tetanus neurotoxins block neurotransmitter release, Biochimie, vol.82, pp.427-446, 2000.

F. A. Meunier, G. Schiavo, and J. Molgo, Botulinum neurotoxins: From paralysis to recovery of functional neuromuscular trasnmission, The Journal of Physiology, vol.96, pp.105-113, 2002.

R. Ratts, C. Trujillo, A. Bharti, J. Vanderspek, R. Harrison et al., A conserved motif in transmembrane helix 1 of diphtheria toxin mediates catalytic domain delivery to the cytosol, Proceedings of the National Academy of Sciences of the United States of America, vol.102, issue.43, pp.15635-15640, 2005.

G. Schiavo, M. Matteoli, and C. Montecucco, Neurotoxins affecting neuroexocytosis, Physiological Reviews, vol.80, pp.717-766, 2000.

W. C. Tucker, T. Weber, and E. R. Chapman, Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs, Science, vol.304, issue.5669, pp.435-438, 2004.

T. Sakaba, A. Stein, R. Jahn, and E. Neher, Distinct kinetic changes in neurotransmitter release after SNARE protein cleavage, Science, vol.309, issue.5733, pp.491-494, 2005.

K. L. Lynch, R. R. Gerona, D. M. Kielar, S. Martens, H. T. Mcmahon et al., Synaptotag min-1 utilizes membrane bending and SNARE binding to drive fusion pore expansion, Molecular Biology of the Cell, vol.19, issue.12, pp.5093-5103, 2008.

R. R. Gerona, E. C. Larsen, J. A. Kowalchyk, and T. F. Martin, The C terminus of SNAP25 is essential for Ca(2+)-dependent binding of synaptotagmin to SNARE complexes, The Journal of Biological Chemistry, vol.275, issue.9, pp.6328-6336, 2000.

J. P. Apland, M. Adler, and G. A. Oyler, Inhibition of neurotransmitter release by peptides that mimic the N-terminal domain of SNAP-25, Journal of Protein Chemistry, vol.22, issue.2, pp.147-153, 2003.

R. Gutierrez, T. Garcia, I. Gonzalez, B. Sanz, P. E. Hernandez et al., A quantitative PCR-ELISA for the rapid enumeration of bacteria in refrigerated raw milk, Journal of Applied Microbiology, vol.83, pp.518-523, 1997.

J. E. Keller and E. A. Neale, The role of the synaptic protein snap-25 in the potency of botulinum neurotoxin type a, The Journal of Biological Chemistry, vol.276, pp.13476-13482, 2001.

Y. A. Chen, S. J. Scales, J. R. Jagath, and R. H. Scheller, A discontinuous SNAP-25 C-terminal coil supports exocytosis, The Journal of Biological Chemistry, vol.276, pp.28503-28508, 2001.

Y. A. Chen, S. J. Scales, S. M. Patel, Y. C. Doung, and R. H. Scheller, SNARE complex formation is triggered by Ca2+ and drives membrane fusion, Cell, vol.97, pp.165-174, 1999.

C. G. Schuette, K. Hatsuzawa, M. Margittai, A. Stein, D. Riedel et al., Determinants of liposome fusion mediated by synaptic SNARE proteins, Proceedings of the National Academy of Sciences of the United States of America, vol.101, issue.9, pp.2858-2863, 2004.

M. Bajohrs, C. Rickman, T. Binz, and B. Davletov, A molecular basis underlying differences in the toxicity of botulinum serotypes A and E, EMBO Reports, vol.5, pp.1090-1095, 2004.

N. Salem, V. Faundez, J. T. Horng, and R. B. Kelly, A v-SNARE participates in synaptic vesicle formation mediated by the AP3 adaptor complex, Nature Neuroscience, vol.1, issue.7, pp.551-556, 1998.

P. Foran, G. W. Lawrence, C. C. Shone, K. A. Foster, and J. O. Dolly, Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chro-maffin cells: Correlation with its blockade of catecholamine release, Biochemistry, vol.35, pp.2630-2636, 1996.

V. V. Vaidyanathan, K. Yoshino, M. Jahnz, C. Dorries, S. Bade et al., Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: Domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage, Journal of Neurochemistry, vol.72, issue.1, pp.327-337, 1999.

M. R. Popoff, C. Mazuet, and B. Poulain, Botulism and Tetanus, The Prokaryotes: Human Microbiology. Human Microbiology. 5, pp.247-290, 2013.

R. Legroux, J. C. Levaditi, and C. Jéramec, Le botulisme en France pendant l'occupation, Presse Médicale, vol.57, pp.109-110, 1947.

K. F. Meyer, The status of botulism as a world health problem, Bulletin of the World Health Organization, vol.15, issue.1-2, pp.281-298, 1956.

M. Sebald and G. Saimot, Le diagnostic biologique du botulisme, Medecine et Maladies Infectieuses, vol.3, pp.83-85, 1973.

M. Sebald, J. Billon, R. Cassaigne, R. Rosset, and G. Poumeyrol, Le botulisme en France. Incidence, mortalité, aliments responsables avec étude des foyers dus à un aliment qui n'est pas de préparation familiale, Med Nut, vol.16, pp.262-268, 1980.

J. P. Carlier, E. Espié, M. R. Popoff, and F. Le-botulisme-en, Bulletin Epidémi ologique Hebdomadaire, pp.281-284, 2003.

J. P. Carlier, C. Henry, V. Lorin, and M. R. Popoff, Le botulisme en France a la fin du deuxième millénaire, Bulletin Epidémiologique Hebdomadaire, vol.9, pp.37-39, 1998.

S. Haeghebaert, M. R. Popoff, J. P. Carlier, G. Pavillon, and E. Delarocque-astagneau, Caracté ristiques épidémiologiques du botulisme humain en France, vol.14, pp.57-59, 1991.

C. Mazuet, J. Silva, N. Legeay, C. Sautereau, J. Michel et al., Bulletin Epidémiologique Hebdomadaire, vol.3, pp.46-54, 2018.

C. Mazuet, P. Bouvet, L. A. King, M. R. Popoff, and F. Le-botulisme-humain-en, Bulletin Epidémiologique Hebdomadaire, vol.6, pp.49-53, 2007.

C. Mazuet, L. A. King, P. Bouvet, C. Legeay, J. Sautereau et al., Bulletin Epidémiologique Hebdomadaire, vol.6, pp.106-114, 2010.

M. Dahlenborg, E. Borch, and P. Radstrom, Development of a combined selection and enrichment PCR procedure for Clostridium botulinum types B, E, and F and its use to determine prevalence in fecal samples from slaughtered pigs, Applied and Environmental Microbiology, vol.67, issue.10, pp.4781-4788, 2001.

J. Myllykoski, M. Nevas, M. Lindstrôm, and H. Korkeala, The detection and prevalence of Clostridium botulinum in pig intestinal samples, International Journal of Food Microbiology, vol.110, issue.2, pp.172-177, 2006.

C. Mazuet, J. Sautereau, C. Legeay, C. Bouchier, P. Bouvet et al., An atypical outbreak of food-borne botulism due to Clostridium botulinum types B and E from ham, Journal of Clinical Microbiology, vol.53, issue.2, pp.722-726, 2014.
URL : https://hal.archives-ouvertes.fr/pasteur-01768473

C. Castor, C. Mazuet, M. Saint-leger, S. Vygen, J. Coutureau et al., Cluster of two cases of botulism due to Clostridium baratii type F in France, Euro Surveillance, vol.20, issue.6, pp.1-3, 2014.
URL : https://hal.archives-ouvertes.fr/pasteur-01780196

C. Mazuet, C. Legeay, J. Sautereau, C. Bouchier, A. Criscuolo et al., Characteriza tion of Clostridium baratii type F strains responsible for an outbreak of botulism linked to beef meat consumption in France, PLOS Currents Outbreaks, 2017.

H. Trehard, I. Poujol, C. Mazuet, Q. Blanc, Y. Gillet et al., A cluster of three cases of botulism due to Clostridium baratii type F, France, Euro Surveillance, vol.21, issue.4, pp.2-5, 2015.
URL : https://hal.archives-ouvertes.fr/pasteur-01783827

C. Mazuet, E. J. Yoon, S. Boyer, S. Pignier, T. Blanc et al., A penicillin-and metronidazole-resistant Clostridium botulinum strain responsible for an infant botulism case, Clinical Microbiology and Infection, vol.22, issue.7, pp.644-651, 2016.
URL : https://hal.archives-ouvertes.fr/pasteur-01325747

B. I. Botulism, The challenge of diagnosis and treatment, Reviews in Neurological Diseases, vol.3, issue.4, pp.182-189, 2006.

D. Akbulut, J. Dennis, M. Gent, K. A. Grant, V. Hope et al., Wound botulism in injectors of drugs: Upsurge in cases in England during, Euro Surveillance, vol.10, issue.9, pp.172-174, 2004.

, Mode of Action, Botulinum Toxins

F. Roblot, M. Popoff, J. P. Carlier, C. Godet, P. Abbadie et al., Botulism in patients who inhale cocaine: The first cases in France, Clinical Infectious Diseases, vol.43, issue.5, pp.51-52, 2006.

C. Mazuet, C. Legeay, J. Sautereau, L. Ma, C. Bouchier et al., Diversity of group I and II Clostridium botulinum strains from France including recently identified subtypes
URL : https://hal.archives-ouvertes.fr/pasteur-01325752

, Genome Biology and Evolution, vol.8, issue.6, pp.1643-1660, 2016.

S. Haeghebaert, J. P. Carlier, and M. R. Popoff, Caractéristiques épidémiologiques du botulisme humain en France, Bulletin Epidémiologique Hebdomadaire, vol.29, pp.129-130, 2001.

M. Sebald and F. Le-botulisme-humain-en, les données du Centre de Référence sur les Anaérobies. Revue D'épidémiologie et de Santé Publique, vol.44, p.47, 1970.

R. Legroux, C. Jeramec, and J. C. Levaditi, Statistique du botulisme de l'occupation 1940-1944. Bulletin de l'Academie de Médecine, vol.129, pp.643-645, 1945.

M. Weinberg, R. Nativelle, and A. R. Prévot, Les Microbes Anaérobies, Masson et Cie; 1937. 1186 p

J. L. Verge and . Botulisme, Recueil De Medecine Veterinaire, vol.127, pp.767-828, 1951.

, Botulinum Toxin, vol.28