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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
; and
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
  • pmid:25015819
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
2016-04-01 10:52:54
date last changed
2022-04-04 22:13:56
@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}},
  doi          = {{10.4049/jimmunol.1401268}},
  volume       = {{193}},
  year         = {{2014}},
}