Immunochemical studies of diphtherial toxin and related nontoxic mutant proteins.

Infection and Immunity
S J CryzR K Holmes

Abstract

Competitive binding radioimmunoassays were used to analyze the immunochemistry of diphtherial toxin. Rabbit antisera obtained by immunization with formolized toxoid or fragment A were used to characterize purified toxin, toxoid, fragment A, and related nontoxic mutant proteins. Antitoxoid serum had a high titer of neutralizing activity. Most of the antibodies in antitoxoid bound to toxin but not to fragment A. The anti-fragment A antibodies that were present in antitoxoid recognized determinants of fragment A that were exposed on unnicked toxin. Formaldehyde treatment partially destroyed antibody-binding sites associated with the A and B domains of toxin. Anti-fragment A serum had a low titer of neutralizing activity. The specificities of the anti-fragment A antibodies in antitoxoid and anti-fragment A sera were different. Approximately half of the anti-fragment A antibodies in anti-fragment A serum recognized determinants of fragment A that were masked in toxin. Per unit of fragment A-binding activity, anti-fragment A serum was significantly more potent than antitoxoid serum as an inhibitor of the enzymatic activity of fragment A. By analyzing the antigenic structure of several nontoxic mutant proteins (cross-reacting material...Continue Reading

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Citations

Apr 1, 1987·Infection and Immunity·A NicosiaR Rappuoli
Mar 1, 1993·Infection and Immunity·J M Rolf, L Eidels
Nov 1, 1985·Annales De L'Institut Pasteur. Microbiology·J E Alouf
Sep 30, 2010·Immunopharmacology and Immunotoxicology·Simona Lucia BavaroDarja Kanduc

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