Biochemical and Biophysical Research Communications
Structural studies on ε-prototoxin of clostridium perfringens type D. Localization of the site of tryptic scission necessary for activation to ε-toxin
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Branching out the aerolysin, ETX/MTX-2 and Toxin_10 family of pore forming proteins
2021, Journal of Invertebrate PathologyCitation Excerpt :The crystal structure of pro-ETX resembles proaerolysin in the pore forming domain (Fig. 3B). The pro-ETX undergoes proteolysis at both the N- and C-terminus to become active (Bhown and Habeeb, 1977; Minami et al., 1997; Worthington and Mulders, 1977). At the organismal level, this active toxin crosses the gut wall of an infected individual by an unknown mechanism (Finnie, 2003).
Etx-Y71A as a non-toxic mutant of Clostridium perfringens epsilon toxin induces protective immunity in mice and sheep
2020, VaccineCitation Excerpt :Epsilon toxin (Etx) produced by Clostridium perfringens toxinotypes B and D is the third most potent clostridial toxin after the botulinum and tetanus neurotoxins, and it is classified as a category B biological agent by USA Centers for Disease Control and Prevention [1–3]. Etx is secreted as a prototoxin that is activated when its N-terminal 11–13 amino acids (AAs) and C-terminal 22–29 AAs are removed by proteases, such as trypsin, chymotrypsin, and γ-protease [4,5]. Etx is associated with fatal enterotoxemia in livestock species, mainly sheep and goats, resulting in considerable economic losses [6–8].
Clostridium perfringens epsilon toxin mutant Y30A-Y196A as a recombinant vaccine candidate against enterotoxemia
2014, VaccineCitation Excerpt :For full activity of the toxin, proteolytic processing is required, with carboxy-terminal and amino-terminal peptides removed. Toxin activation typically occurs in the gut either by digestive proteases of the host, such as trypsin and chymotrypsin [8], or by λ-protease produced by C. perfringens itself [9,10]. To prevent Etx-induced enterotoxemia in domesticated livestock, a number of commercial vaccines are available that have been used extensively over the past decades.
Attack of the nervous system by clostridium perfringens epsilon toxin: From disease to mode of action on neural cells
2013, ToxiconCitation Excerpt :Removal of the 11 N-terminal (or the 13 N-terminal) and of the 29 C-terminal residues amino-acids by proteases (notably the α-chymotrypsin, trypsin and λ-protease) converts the inactive protoxin (proET) into a fully active form (i.e. the toxin, ET 28.6 kDa), with a lethal dose (LD) of about 70 ng kg−1 in mice (i.e. 400,000 mouse-LD per mg protein) (Minami et al., 1997; reviewed by Popoff, 2011a). Proteases involved in conversion of proET into ET are synthesized by C. perfringens (Minami et al., 1997) as well as by the host (Bhown and Habeerb, 1977; Worthington and Mülders, 1977). The 3D structure of ET has been resolved and presents similarities with the pore-forming toxin aerolysin produced by Aeromonas hydrophila species (Cole et al., 2004; Gurcel et al., 2006; Parker et al., 1994).
Expression and purification of functional Clostridium perfringens alpha and epsilon toxins in Escherichia coli
2011, Protein Expression and PurificationCitation Excerpt :The epsilon toxin (ETX), which is produced by type B and D strains, is a potent neurotoxin and can lead to fatal illness (enterotoxemia) in a variety of livestock animals, most frequently in sheep. ETX is expressed and secreted as a precursor (prototoxin) [6], which is activated upon protease-mediated cleavage of short peptides from both the amino and the carboxyl termini [7–9]. Among the tested cell lines, only Madin-Darby canine kidney (MDCK) cells and, to a lesser extent, human leiomyoblastoma cells (G-402) are sensitive to ETX [10–12].
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Present Address: Department of Biochemistry and Nutrition University of Puerto Rico, Medical Science Campus G.P.O. Box 5067 San Juan, Puerto Rico, 58936