Immunochemical characterization of cell wall protein antigen purified from the cell wall autolysate of Clostridium botulinum type A.
The cell wall protein antigen was solubilized from the isolated cell walls of Clostridium botulinum type A by autolysis and purified by diethylaminoethyl-cellulose column chromatography followed by gel filtration on Sephadex G-150. The two fractions showed a high degree of the serological activity and produced a main fused precipitin line in immunodiffusion tests against the homologous antiserum. The fact that antigenic fractions contained various kinds of amino acids but no detectable amounts of amino sugars or carbohydrates suggests that the antigens were principally composed of proteins. The protein antigen possessed multiple antigenic components in immunoelectrophoresis. As serological activity, the antigen was heat-stable and resistant to tryptic digestion but sensitive to the actions of pronase, nagarse or pepsin. The protein antigen appeared to be responsible for the common antigenicity among the proteolytic strains of C. botulinum.
D000942:Antigens, Bacterial / Q000032:analysis / Q000302:isolation & purification*; D001426:Bacterial Proteins / Q000032:analysis / Q000276:immunology*; D002473:Cell Wall / Q000276:immunology; D003014:Clostridium botulinum / Q000276:immunology*; D000939:Epitopes
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D000939:Epitopes