Study of Toxic and Antigenic Structures of Botulinum Neurotoxin
Abstract
Procedure to purify types A, B, and E neurotoxin (NT) using FPLC was developed. The NT produced by strain B-657 was identified and characterized based on partial amino acid sequence. The heavy chains of types A, B and E NTs were enzymatically cleaved at about the mid-point. The two halves of the heavy chain of type A were isolated and partially sequenced. Specific chemical modification reactions were used to examine the role of carboxyl groups, lysine and tyrosine residues. Type B and E NTs completely detoxified following tyrosine modification were used as immunogen to raise, in rabbits, NT neutralizing antibody. Conformation of the NTs and the isolated heavy and light chains were examined by circular dichroism, fluorescence spectra and UV-difference spectra. Interaction of the subunit chains of the three NTs with lipid bilayer surface was examined. Keywords: Clostridium botulinum; Amino acid sequence. (AW)
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 17, 1988
- Accession Number
- ADA202891
Entities
People
- B. R. Dasgupta
Organizations
- University of Wisconsin–Madison