Accession Number:

ADA386484

Title:

Light Chain of Botulinum A Neurotoxin Expressed as an Inclusion Body from a Synthetic Gene is Catalytically and Functionally Active

Descriptive Note:

Journal article

Corporate Author:

ARMY MEDICAL RESEARCH INST OF INFECTIOUS DISEASES FORT DETRICK MD

Personal Author(s):

Report Date:

2000-01-01

Pagination or Media Count:

14.0

Abstract:

Botulinum neurotoxins, the most potent of all toxins, induce lethal neuromuscular paralysis by inhibiting exocytosis at the neuromuscular junction. The light chains LC of these dichain neurotoxins are a new class of zinc-endopeptidases that specifically cleave the synaptosomal proteins, SNAP-25, VAMP, or syntaxin at discrete sites. To facilitate the structural and functional characterization of these unique endopeptidases, we constructed a synthetic gene for the LC of the botulinum neurotoxin serotype A BoNTA, overexpressed it in Escherichia coli, and purified the gene product from inclusion bodies. Our procedure can provide 1.1g of the LC from 1 L of culture. The LC product was stable in solution at 4 C for at least 6 months.

Subject Categories:

  • Biochemistry
  • Pharmacology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE