Limited digestion of staphylococcal enterotoxin B (SEB) with trypsin resulted in the generation of a 12-Kda amino-terminal fragment and a 17-Kda carboxy-terminal fragment which were isolated by preparative iso-electric focusing. The carboxy-terminal fragment exhibited significant mitogenic activity for murine splenocytes, whereas the isolated amino-terminal fragment possessed little detectable mitogenic activity. Monoclonal antibodies (MAbs) specific for the carboxy-terminal fragment neutralised most of the mitogenic activity of both the intact toxin and the carboxy-terminal fragment. MAbs specific for the amino-terminal fragment had no detectable neutralising activity. These results support the hypothesis that the epitope(s) responsible for mitogenic activity is located in the carboxy-terminal region of SEB.


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