Study of Toxic and Antigenic Structures of Botulinum Neurotoxin
Annual rept. 15 Sep 1984-14 Sep 1985
WISCONSIN UNIV-MADISON FOOD RESEARCH INST
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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.