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

In English

Författare

Summary, in English

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.

Publiceringsår

2014

Språk

Engelska

Sidor

1998-2004

Publikation/Tidskrift/Serie

Journal of Immunology

Volym

193

Issue

4

Dokumenttyp

Artikel i tidskrift

Förlag

American Association of Immunologists

Ämne

  • Immunology in the medical area

Status

Published

Forskningsgrupp

  • Medical Structural Biology

ISBN/ISSN/Övrigt

  • ISSN: 1550-6606