Expression and purification of Clostridium perfringens beta-toxin glutathione S-transferase fusion protein

FEMS Microbiol Lett. 1995 Aug 1;130(2-3):273-8. doi: 10.1111/j.1574-6968.1995.tb07731.x.

Abstract

The beta-toxin gene from Clostridium perfringens type C was cloned and expressed as a glutathione S-transferase fusion protein in Escherichia coli. The DNA sequence was determined and compared to the type B sequence. Two nucleotide differences were found in the protein coding sequence, resulting in one amino acid difference between the two proteins. The purified beta-toxin fusion protein is not toxic in mice, but rabbit antiserum raised against it neutralises the toxic effect of C. perfringens type C culture filtrate in mice.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Toxins / biosynthesis*
  • Bacterial Toxins / genetics
  • Bacterial Toxins / immunology
  • Base Sequence
  • Clostridium perfringens / pathogenicity*
  • Glutathione Transferase / biosynthesis*
  • Molecular Sequence Data
  • Open Reading Frames
  • Recombinant Fusion Proteins / biosynthesis*

Substances

  • Bacterial Toxins
  • CPB protein, Clostridium perfringens
  • Recombinant Fusion Proteins
  • Glutathione Transferase

Associated data

  • GENBANK/X83275