Structure of the Superantigen Staphylococcal Enterotoxin B in Complex with TCR and Peptide-MHC Demonstrates Absence of TCR-Peptide Contacts.

Karin Rödström, Karin Elbing, Karin Lindkvist

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

35 Citeringar (SciVal)

Sammanfattning

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 β-chain of TCR, allowing for an interaction between the α-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.
Originalspråkengelska
Sidor (från-till)1998-2004
TidskriftJournal of Immunology
Volym193
Utgåva4
DOI
StatusPublished - 2014

Ämnesklassifikation (UKÄ)

  • Immunologi inom det medicinska området

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