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

Rödström, Karin LU ; Elbing, Karin LU and Lindkvist, Karin LU (2014) In Journal of Immunology 193(4). p.1998-2004
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Immunology
volume
193
issue
4
pages
1998 - 2004
publisher
American Association of Immunologists
external identifiers
  • pmid:25015819
  • wos:000341139300049
  • scopus:84905973851
ISSN
1550-6606
DOI
10.4049/jimmunol.1401268
language
English
LU publication?
yes
id
9603373f-5e40-4f9c-95b3-368308a7877b (old id 4582450)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/25015819?dopt=Abstract
date added to LUP
2014-08-07 22:35:42
date last changed
2017-11-12 03:13:21
@article{9603373f-5e40-4f9c-95b3-368308a7877b,
  abstract     = {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.},
  author       = {Rödström, Karin and Elbing, Karin and Lindkvist, Karin},
  issn         = {1550-6606},
  language     = {eng},
  number       = {4},
  pages        = {1998--2004},
  publisher    = {American Association of Immunologists},
  series       = {Journal of Immunology},
  title        = {Structure of the Superantigen Staphylococcal Enterotoxin B in Complex with TCR and Peptide-MHC Demonstrates Absence of TCR-Peptide Contacts.},
  url          = {http://dx.doi.org/10.4049/jimmunol.1401268},
  volume       = {193},
  year         = {2014},
}