High level expression, purification and immunogenicity analysis of a protective recombinant protein against botulinum neurotoxin type E

World J Microbiol Biotechnol. 2014 Jun;30(6):1861-7. doi: 10.1007/s11274-014-1609-0. Epub 2014 Jan 29.

Abstract

Botulinum neurotoxin type E heavy chain consists of two domains: N-terminal half as a translocation domain and C-terminal half (Hcc) as a binding domain. In this research a synthetic gene fragment encoding the binding domain of botulinum neurotoxin type E (BoNT/E-Hcc) was highly expressed in Escherichia coli by pGEX4T-1 vector. After purification, the recombinant BoNT/E-Hcc was evaluated by SDS-PAGE and western blot (immunoblot) analysis. Average yields obtained in this research were 3.7 mg recombinant BoNT/E-Hcc per liter of bacterial culture. The recombinant protein was injected in mice for study of its protection ability against botulinum neurotoxin type E challenges. The challenge studies showed that, vaccinated mice were fully protected against 10⁴ × minimum lethal dose of botulinum neurotoxin type E.

MeSH terms

  • Animals
  • Bacterial Vaccines / genetics
  • Bacterial Vaccines / immunology
  • Bacterial Vaccines / isolation & purification
  • Botulinum Toxins / genetics
  • Botulinum Toxins / immunology*
  • Botulinum Toxins / isolation & purification
  • Botulism / immunology
  • Botulism / microbiology
  • Botulism / prevention & control*
  • Clostridium botulinum / genetics
  • Clostridium botulinum / immunology
  • Clostridium botulinum / physiology
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Humans
  • Male
  • Mice
  • Mice, Inbred BALB C
  • Recombinant Proteins / genetics
  • Recombinant Proteins / immunology
  • Recombinant Proteins / isolation & purification

Substances

  • Bacterial Vaccines
  • Recombinant Proteins
  • Botulinum Toxins
  • botulinum toxin type E