Monoclonal antibodies to staphylococcal enterotoxins B and C: cross-reactivity and localization of epitopes on tryptic fragments.

Murine monoclonal antibodies reactive with staphylococcal enterotoxins B (SEB) and C1 (SEC1) were isolated by hybridoma techniques. Of the nine antibodies, three reacted only with SEB, two reacted with SEB and SEC1, three reacted with all subtypes of SEC, and one reacted only with SEC2 and SEC3. All of the antibodies reacted with protein blotted onto nitrocellulose from electrophoresis gels which corresponded to the enterotoxin band. Fragments of SEB and SEC1 were generated by limited digestion of the toxin with trypsin. With the immunoblot technique, four of the five antibodies reactive with SEB reacted with the tryptic fragment of molecular weight 17,000, and the five antibodies reactive with SEC1 reacted with the tryptic fragment of molecular weight 14,000.