1997
DOI: 10.1016/s0378-1119(97)00493-9
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Beta2 toxin, a novel toxin produced by Clostridium perfringens

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Cited by 269 publications
(312 citation statements)
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“…In animals, the b2-toxin causes a severe, often fatal form of hemorrhagic enteritis (Gibert et al 1997;Manteca et al 2002). In our study, we found that hemorrhagic enteritis in cattle can be caused by both lineage III strains and certain lineage I strains, but the b2-toxin occurs only among lineage I strains.…”
Section: Discussionmentioning
confidence: 46%
See 1 more Smart Citation
“…In animals, the b2-toxin causes a severe, often fatal form of hemorrhagic enteritis (Gibert et al 1997;Manteca et al 2002). In our study, we found that hemorrhagic enteritis in cattle can be caused by both lineage III strains and certain lineage I strains, but the b2-toxin occurs only among lineage I strains.…”
Section: Discussionmentioning
confidence: 46%
“…Pathogenic strains of C. perfringens cause a variety of human and animal diseases including food poisoning, antibiotic-associated diarrhea, gas gangrene, necrotic enteritis, necrotizing colitis, sudden death syndrome, and enterotoxemia (Lindsay 1996;Songer 1996;Gibert et al 1997;Rood 1998;Brynestad and Granum 2002;Bos et al 2005). C. perfringens causes this wide array of diseases as a result of being able to produce at least 15 toxins (Rood 1998;Petit et al 1999;Smedley et al 2004).…”
mentioning
confidence: 99%
“…The beta toxin induces hemorrhagic necrosis of the intestinal mucosa (Lawrence & Cooke, 1980;Gilbert et al, 1997). Although the exact mechanism of action is not yet known, beta 1 toxin is most likely also a membrane-damaging toxin.…”
Section: Perfringens Virulence Factorsmentioning
confidence: 99%
“…Almost a decade ago, the beta2 toxin and its encoding gene (cpb2) were first identified in C. perfringens type C (strain CWC245) isolated from a piglet with necrotizing enterocolitis (8). The amino acid sequence of cpb2 showed no significant homologies with cpb from the beta toxin (15%) or other known proteins (8,9).…”
Section: Introductionmentioning
confidence: 99%
“…The amino acid sequence of cpb2 showed no significant homologies with cpb from the beta toxin (15%) or other known proteins (8,9). Although its biological activity was similar to that of the beta toxin it may possess weaker cytotoxic activity (8). A possible pore formation or other mechanisms leading to cell membrane disruption appear to be its most plausible function (1).…”
Section: Introductionmentioning
confidence: 99%