Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC‐IIα

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<jats:title>Abstract</jats:title><jats:p>Staphylococcal enterotoxins (SEs) are superantigenic protein toxins responsible for a number of life‐threatening diseases. The X‐ray structure of a staphylococcal enterotoxin A (SEA) triple‐mutant (L48R, D70R, and Y92A) vaccine reveals a cascade of structural rearrangements located in three loop regions essential for binding the α subunit of major histocompatibility complex class II (MHC‐II) molecules. A comparison of hypothetical model complexes between SEA and the SEA triple mutant with MHC‐II HLA‐DR1 clearly shows disruption of key ionic and hydrophobic interactions necessary for forming the complex. Extensive dislocation of the disulfide loop in particular interferes with MHC‐IIα binding. The triple‐mutant structure provides new insights into the loss of superantigenicity and toxicity of an engineered superantigen and provides a basis for further design of enterotoxin vaccines.</jats:p>

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