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Nonconserved residues of staphylococcal enterotoxin C1 (SEC1) were converted to their counterparts in SEC2. The mutants that resulted were examined for reactivity with monoclonal antibodies (MAbs). Substitution at position 20, 22, or 26 interfered with binding of an SEC1-specific MAb. SEC1 mutants with substitutions at all three positions reacted only with an SEC2-specific MAb. Antibody-binding patterns were not associated with isoelectric point differences. All mutants retained biological activity.

Residues 20, 22, and 26 determine the subtype specificities of staphylococcal enterotoxins C1 and C2