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Staphylococcus aureus, a common pathogenic bacteria, produces several super antigenic virulence factors known as staphylococcal enterotoxins. Of these heat-resistant enterotoxins, staphylococcal enterotoxin B (SEB), a 28 kDa protein consisting of 239 amino acids, has been of particular interest because it is one of the most common causes of foodborne illnesses, toxic shock syndrome, and a potential bioterrorism and biowarfare threat. The structure of SEB consists of two distinct domains including an N-terminal, β-barrel-like domain and a C-terminal domain rich in α-helices and containing a β-grasp motif. The toxicity of SEB is mediated through its interaction with the major histocompatibility complex (MHC) class II on target cells resulting in widespread proliferation of leukocytes and cytokine release.