Purification and characterization of a cytotonic protein expressed In vitro by the live cholera vaccine candidate CVD 103-HgR

Infect Immun. 2000 Oct;68(10):6062-5. doi: 10.1128/IAI.68.10.6062-6065.2000.

Abstract

Cholera vaccines developed by the deletion of CTX genes from Vibrio cholerae induce a residual reactogenicity in up to 10% of vaccinees. A novel cytotonic agent named secreted CHO cell elongating protein (S-CEP) was purified from culture supernatants of CVD 103-HgR (Levine et al., Lancet ii:467-470, 1988). Five fractionation steps yielded electrophoretically pure S-CEP with an M(r) of 79,000. A partially purified preparation caused fluid accumulation in the sealed infant mouse model. The amino terminus bore a unique sequence with strong homology to a cytotonic toxin of El Tor V. cholerae.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / isolation & purification*
  • Bacterial Toxins / metabolism
  • Bacterial Toxins / toxicity
  • CHO Cells
  • Cholera Vaccines
  • Cricetinae
  • Mice
  • Molecular Sequence Data
  • Vibrio cholerae / growth & development
  • Vibrio cholerae / metabolism*
  • Vibrio cholerae / pathogenicity*

Substances

  • Bacterial Toxins
  • Cholera Vaccines