The α-toxin produced by the type strain of (NCTC 8237) was shown to differ from the α-toxins produced by most strains of isolated from man and from calves with respect to reactivity with a neutralizing monoclonal antibody (DY2F5D11). The difference in antibody binding correlated with three differences in the deduced amino acid sequence (Ala to Asp; Thr to Ala; Ser to Pro) of the α-toxins. Using octapeptides synthesized on the basis of the amino acid sequences from these regions of variability, it was shown that the Ala to Asp change had the greatest effect on reducing the binding of monoclonal antibody DY2F5D11 to the α-toxin. These differences did not affect the enzymic or toxic properties of the protein. However, the phospholipase C activity of the α-toxin produced by strain NCTC 8237 was more susceptible to inactivation by chymotrypsin. The changes in amino acid sequence did not affect the ability of a C-terminal domain vaccine, derived from the α-toxin of strain NCTC 8237, to induce protection against the α-toxin from a bovine enteric strain of


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