Study of Toxic and Antigenic Structures of Botulinum Neurotoxin
Abstract
The neurotoxin (NT) from type B, strain 657, has been partially purified. Lysine and tyrosine residues in type A and E NT were selectively modified to study their roles in toxicity and antigenicity. A large number of lysine residues were not critical for toxicity. Integrity of tyrosine residue(s) were critical for toxigenic structures but not for serological reactivity. Type E NT completely detoxified following modification of tyrosine residues proved to be a good immunogen (second generation toxoid). Antiserum raised in rabbits neutralized the NT. The heavy chain of type A NT was enzymatically fragmented into two halves and partially sequenced. The conformation of the single chain type E NT appeared more unfolded when it was nicked to the dichain form.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 04, 1986
- Accession Number
- ADA175272
Entities
People
- B. R. Dasgupta
Organizations
- University of Wisconsin–Madison