Publication Abstract from PubMed
Superantigens are immune-stimulatory toxins produced by Staphylococcus aureus, which are able to interact with host immune receptors to induce a massive release of cytokines, causing toxic shock syndrome and possibly death. In this article, we present the x-ray structure of staphylococcal enterotoxin B (SEB) in complex with its receptors, the TCR and MHC class II, forming a ternary complex. The structure, in combination with functional analyses, clearly shows how SEB adopts a wedge-like position when binding to the beta-chain of TCR, allowing for an interaction between the alpha-chain of TCR and MHC. Furthermore, the binding mode also circumvents contact between TCR and the peptide presented by MHC, which enables SEB to initiate a peptide-independent activation of T cells.
Structure of the Superantigen Staphylococcal Enterotoxin B in Complex with TCR and Peptide-MHC Demonstrates Absence of TCR-Peptide Contacts.,Rodstrom KE, Elbing K, Lindkvist-Petersson K J Immunol. 2014 Jul 11. pii: 1401268. PMID:25015819[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
