Accession Number:

ADA175272

Title:

Study of Toxic and Antigenic Structures of Botulinum Neurotoxin

Descriptive Note:

Annual rept. 15 Sep 1984-14 Sep 1985

Corporate Author:

WISCONSIN UNIV-MADISON FOOD RESEARCH INST

Personal Author(s):

Report Date:

1986-02-04

Pagination or Media Count:

10.0

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 residues 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.

Subject Categories:

  • Biochemistry
  • Toxicology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE