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Molecular basis of toxicity of Clostridium perfringens epsilon toxin

Bokori‐Brown, Monika ; Savva, Christos G. ; Fernandes da Costa, Sérgio P. ; Naylor, Claire E. ; Basak, Ajit K. ; Titball, Richard W.

The FEBS journal, 2011-12, Vol.278 (23), p.4589-4601 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

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  • Título:
    Molecular basis of toxicity of Clostridium perfringens epsilon toxin
  • Autor: Bokori‐Brown, Monika ; Savva, Christos G. ; Fernandes da Costa, Sérgio P. ; Naylor, Claire E. ; Basak, Ajit K. ; Titball, Richard W.
  • Assuntos: Animals ; Bacterial Toxins - chemistry ; Bacterial Toxins - metabolism ; Bacterial Toxins - toxicity ; Clostridium perfringens - metabolism ; Clostridium perfringens ; crystal structure ; enterotoxaemia ; epsilon toxin ; Humans ; Models, Molecular ; pore‐forming ; Protein Conformation ; Rats ; Synaptosomes - metabolism
  • É parte de: The FEBS journal, 2011-12, Vol.278 (23), p.4589-4601
  • Descrição: Clostridium perfringensε‐toxin is produced by toxinotypes B and D strains. The toxin is the aetiological agent of dysentery in newborn lambs but is also associated with enteritis and enterotoxaemia in goats, calves and foals. It is considered to be a potential biowarfare or bioterrorism agent by the US Government Centers for Disease Control and Prevention. The relatively inactive 32.9 kDa prototoxin is converted to active mature toxin by proteolytic cleavage, either by digestive proteases of the host, such as trypsin and chymotrypsin, or by C. perfringensλ‐protease. In vivo, the toxin appears to target the brain and kidneys, but relatively few cell lines are susceptible to the toxin, and most work has been carried out using Madin–Darby canine kidney (MDCK) cells. The binding of ε‐toxin to MDCK cells and rat synaptosomal membranes is associated with the formation of a stable, high molecular weight complex. The crystal structure of ε‐toxin reveals similarity to aerolysin from Aeromonas hydrophila, parasporin‐2 from Bacillus thuringiensis and a lectin from Laetiporus sulphureus. Like these toxins, ε‐toxin appears to form heptameric pores in target cell membranes. The exquisite specificity of the toxin for specific cell types suggests that it binds to a receptor found only on these cells. Clostridium perfringensε‐toxin is the etiologic agent of enterotoxaemia and appears to target the brain and kidneys. The crystal structure of ε‐toxin reveals similarity to aerolysin from Aeromonas hydrophila, parasporin‐2 from Bacillus thuringiensis, and a lectin from Laetiporus sulphurous. Like these toxins, ε‐toxin forms pores in target cell membranes, but differs from these toxins because of its high specificity and potency
  • Editor: Oxford, UK: Blackwell Publishing Ltd
  • Idioma: Inglês
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