Isolation of botulinolysin, a thiol-activated hemolysin, from serotype D Clostridium botulinum: A species-specific gene duplication in Clostridia.

@article{Suzuki2016IsolationOB,
  title={Isolation of botulinolysin, a thiol-activated hemolysin, from serotype D Clostridium botulinum: A species-specific gene duplication in Clostridia.},
  author={Tomonori Suzuki and Thomas Nagano and Koichi Niwa and Shingo Mutoh and Masataka Uchino and Motohiro Tomizawa and Yoshimasa Sagane and Toshihiro Watanabe},
  journal={Microbiological research},
  year={2016},
  volume={193},
  pages={
          20-29
        }
}

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TLDR
The purified hemolysin had a lethal effect in mice and was cytotoxic for some cultured cells: its 50% lethal dose in mice was 310 ng, and the 50% cytot toxic dose for Vero cells was 120 ng/ml.
Molecular Characterization of GroES and GroEL Homologues from Clostridium botulinum
TLDR
Southern and Northern blot analyses indicate that the groESL operon is encoded on the genomic DNA of D-4947 as a single copy, and not on that of its specific toxin-converting phage.
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TLDR
A new method is established to separate the unique D-4947 NT from the complex, which will yield valuable information on structure of botulinum toxin, which is indistinguishable from the parent L-TC with respect to toxicity, hemagglutination activity and gel filtration profile.
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The current state of knowledge of the phylogenetics of the species Cl. botulinum and its neurotoxins is reviewed, and a view is presented that a nomenclature based rigidly on BoNT production is no longer tenable.
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Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine
TLDR
The deduced amino acid sequence of alveolysin shows that alveolarsin shares homologies with listeriolysin O, perfringolysin O, pneumolysin, and streptolysinO, and a single cysteine in the conserved peptide sequence ECTGLA WEWWR.
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