Structural Studies on Intact Clostridium Botulinum Neurotoxins Complexed with Inhibitors Leading to Drug Design

Abstract

In this third annual report we present our progress on two different areas. We have identified two ganglioside binding sites in tetanus toxin. While one is common to botulinum toxins, the other is unique for tetanus. The second unique site also binds a tri-peptide which suggests that this peptide could be used as an inhibitor for tetanus, at least. We have determined the structure of the C fragment of botulinum neurotoxin type B. We have identified a number of inactive mutants of BoNT/E-LC. Some of these mutants may be potential candidates for vaccines. Most importantly, for the first time we have shown that Glu335Gln mutant of BoNT/E-LC is an apoenzyme devoid of zinc.

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Document Details

Document Type
Technical Report
Publication Date
Feb 01, 2005
Accession Number
ADA432038

Entities

People

  • Subramanyam Swaminathan

Organizations

  • Brookhaven National Laboratory

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Apoproteins
  • Biochemistry
  • Biomedical And Dental Materials
  • Carbohydrates
  • Chemistry
  • Crystal Structure
  • Electron Density
  • Inhibitors
  • Mass Spectrometry
  • Medical Personnel
  • Molecules
  • Polymeric Films
  • Proteins
  • Sialic Acids
  • Small Molecules
  • Three Dimensional

Fields of Study

  • Biology

Readers

  • Microbial Pathology
  • Molecular and Cellular Biochemistry

Technology Areas

  • Biotechnology