Clostridium perfringens enterotoxin and C. perfringens food poisoning, Encyclopedia of Food Microbiology ,
, , pp.438-444, 1999.
Clostridium perfringens enterotoxin: Action, genetics, and translational applications, Toxins, vol.8, p.73, 2016. ,
Expansion of the Clostridium perfringens toxin-based typing scheme, Anaerobe, 2018. ,
Clostridium perfringens type E animal enteritis isolates with highly conserved, silent enterotoxin gene sequences, Infect. Immun, vol.66, pp.4531-4536, 1998. ,
Identification of novel Clostridium perfringens type e strains that carry an iota toxin plasmid with a functional enterotoxin gene, PLoS ONE, vol.6, 2011. ,
Clostridium perfringens sporulation and sporulation-associated toxin production ,
Claudins and the modulation of tight junction permeability, Physiol. Rev, vol.93, pp.525-569, 2013. ,
Multifaceted role of Rho, Rac, Cdc42 and ras in intercellular junctions, lessons from toxins, Biochim. Biophys. Acta, vol.1788, pp.797-812, 2009. ,
Claudin interactions in and out of the tight junction ,
Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein, FEBS Lett, vol.476, pp.258-261, 2000. ,
Specificity of interaction between Clostridium perfringens enterotoxin and claudin-family tight junction proteins, Toxins, vol.2, pp.1595-1611, 2010. ,
Targeting and alteration of tight junctions by bacteria and their virulence factors such as Clostridium perfringens enterotoxin, Pflugers Arch, vol.469, pp.77-90, 2017. ,
The complex interactions between Clostridium perfringens enterotoxin and epithelial tight junctions, Toxicon, vol.39, pp.1781-1791, 2001. ,
Claudins in intestines: Distribution and functional significance in health and diseases ,
Clostridium perfringens type A enterotoxin damages the rabbit colon, Infect. Immun, vol.82, pp.2211-2218, 2014. ,
The interaction of Clostridium perfringens enterotoxin with receptor claudins, Anaerobe, vol.41, pp.18-26, 2016. ,
Towards an understanding of the role of Clostridium perfringens toxins in human and animal disease, Future Microbiol, vol.9, pp.361-377, 2014. ,
Use of Clostridium perfringens enterotoxin and the enterotoxin receptor-binding domain (c-cpe) for cancer treatment: Opportunities and challenges, J. Toxicol, 2012. ,
Compositional and stoichiometric analysis of Clostridium perfringens enterotoxin complexes in caco-2 cells and claudin 4 fibroblast transfectants, Cell. Microbiol, vol.9, pp.2734-2755, 2007. ,
Mechanism of Clostridium perfringens enterotoxin interaction with claudin-3/-4 protein suggests structural modifications of the toxin to target specific claudins, J. Biol. Chem, vol.287, pp.1698-1708, 2012. ,
Clostridium perfringens enterotoxin interacts with claudins via electrostatic attraction, J. Biol. Chem, vol.285, pp.401-408, 2010. ,
Death pathways activated in caco-2 cells by Clostridium perfringens enterotoxin, Infect. Immun, vol.71, pp.4260-4270, 2003. ,
In colon epithelia, Clostridium perfringens enterotoxin causes focal leaks by targeting claudins which are apically accessible due to tight junction derangement, J. Infect. Dis, vol.217, pp.147-157, 2017. ,
Specific binding of Clostridium perfringens enterotoxin fragment to claudin-b and modulation of zebrafish epidermal barrier, Exp. Dermatol, vol.24, pp.605-610, 2015. ,
Clostridium perfringens enterotoxin fragment removes specific claudin from tight junction strands: Evidence for direct involvement of claudin in tight junction barrier, J. Cell Biol, vol.147, pp.195-204, 1999. ,
Structural basis for disruption of claudin assembly in tight junctions by an enterotoxin, Sci. Rep, vol.6, 2016. ,
Structure of the food-poisoning Clostridium perfringens enterotoxin reveals similarity to the aerolysin-like pore-forming toxins, J. Mol. Biol, vol.413, pp.138-149, 2011. ,
Crystal structure of Clostridium perfringens enterotoxin displays features of beta-pore-forming toxins, J. Biol. Chem, vol.286, 2011. ,
Identification of a prepore large-complex stage in the mechanism of action of Clostridium perfringens enterotoxin, Infect. Immun, vol.75, pp.2381-2390, 2007. ,
Cysteine-scanning mutagenesis supports the importance of Clostridium perfringens enterotoxin amino acids 80 to 106 for membrane insertion and pore formation, Infect. Immun, vol.80, pp.4078-4088, 2012. ,
Clostridium perfringens type A enterotoxin forms mepacrine-sensitive pores in pure phospholipid bilayers in the absence of putative receptor proteins, Biochim. Biophys. Acta, vol.1515, pp.38-43, 2001. ,
Enterotoxin of Clostridium perfringens type A forms ion-permeable channels in a lipid bilayer membrane, Biochem. Biophys. Res. Commun, vol.156, pp.551-556, 1988. ,
Cationic currents induced by Clostridium perfringens type a enterotoxin in human intestinal caco-2 cells, J. Med. Microbiol, vol.48, pp.235-243, 1999. ,
The cell wall porin of Nocardia farcinica: Biochemical identification of the channel-forming protein and biophysical characterization of the channel properties, Mol. Microbiol, vol.29, pp.139-150, 1998. ,
Characterization of the channel formed by the mycobacterial porin in lipid bilayer membranes. Demonstration of voltage gating and of negative point charges at the channel mouth, J. Biol. Chem, vol.268, pp.6234-6240, 1993. ,
Adenylate cyclase toxin (cyaa) of Bordetella pertussis. Evidence for the formation of small ion-permeable channels and comparison with hlya of Escherichia coli, J. Biol. Chem, vol.269, pp.27231-27239, 1994. ,
Flow cytometric assay for cytotoxic activity of crude Clostridium perfringens enterotoxin using non-adherent cell fm3a, FEMS Immunol. Med. Microbiol, vol.12, pp.239-244, 1995. ,
Clostridium perfringens epsilon-toxin induces a rapid change in cell membrane permeability to ions and forms channels in artificial lipid bilayers, J. Biol. Chem, vol.276, pp.15736-15740, 2001. ,
URL : https://hal.archives-ouvertes.fr/pasteur-01811229
Solute uptake through bacterial outer membrane, Bacterial Cell Wall ,
, , pp.397-423, 1994.
Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli, Biochim. Biophys. Acta, vol.551, pp.238-247, 1979. ,
Pore formation by the Escherichia coli hemolysin: Evidence for an association-dissociation equilibrium of the pore-forming aggregates, Infect. Immun, vol.57, pp.887-895, 1989. ,
Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes, J. Biol. Chem, vol.269, pp.16706-16711, 1994. ,
Clostridium perfringens ?-toxin shows structural similarity to the pore-forming toxin aerolysin, Nat. Struct. Mol. Biol, vol.11, pp.797-798, 2004. ,
Pore-forming activity of clostridial binary toxins, Biochim. Biophys. Acta, vol.1858, pp.512-525, 2016. ,
URL : https://hal.archives-ouvertes.fr/pasteur-01798115
Anthrax toxin protective antigen: Inhibition of channel function by chloroquine and related compounds and study of binding kinetics using the current noise analysis, Biophys. J, vol.88, pp.1715-1724, 2005. ,
The effect of discrete charges on the electrical properties of a membrane. I, J. Theor. Biol, vol.55, pp.13-27, 1975. ,
Clostridial pore-forming toxins: Powerful virulence factors, Anaerobe, vol.30, pp.220-238, 2014. ,
URL : https://hal.archives-ouvertes.fr/pasteur-01797567
Molecular mechanism of pore formation by aerolysin-like proteins, Philos. Trans. R. Soc. Lond. B Biol. Sci, vol.372, 2017. ,
Identification of the channel-forming domain of Clostridium perfringens epsilon-toxin (etx), Biochim. Biophys. Acta, vol.1788, pp.2584-2593, 2009. ,
Aerolysin of Aeromonas sobria: Evidence for the formation of ion-permeable channels and comparison with alpha-toxin of Staphylococcus aureus, Infect. Immun, vol.58, pp.2127-2132, 1990. ,
Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore, Science, vol.274, pp.1859-1866, 1996. ,
Molecular basis of toxicity of Clostridium perfringens epsilon toxin, FEBS J, vol.278, pp.4589-4601, 2011. ,
Cytotoxicity of Clostridium septicum alpha-toxin: Its oligomerization in detergent resistant membranes of mammalian cells, Microb. Pathog, vol.37, pp.279-286, 2004. ,
Clostridium septicum alpha-toxin forms pores and induces rapid cell necrosis, vol.55, pp.61-72, 2010. ,
URL : https://hal.archives-ouvertes.fr/pasteur-01509604
Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism, Nat. Chem. Biol, vol.9, pp.623-629, 2013. ,
Structure of a C. perfringens enterotoxin mutant in complex with a modified claudin-2 extracellular loop 2, J. Mol. Biol, vol.426, pp.3134-3147, 2014. ,
URL : https://hal.archives-ouvertes.fr/pasteur-01767861
Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli, Biochim. Biophys. Acta, vol.511, pp.305-319, 1978. ,
Clostridium perfringens epsilon-toxin acts on mdck cells by forming a large membrane complex, J. Bacteriol, vol.179, pp.6480-6487, 1997. ,