Advanced

The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation

Saline, Maria; Rodstrom, Karin E. J.; Fischer, Gerhard; Orekhov, Vladislav Yu.; Karlsson, B. Goran and Lindkvist, Karin LU (2010) In Nature Communications 1.
Abstract
Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable beta-domain of TCR (TCRV beta). They induce a massive release of cytokines, which can lead to diseases such as food poisoning and toxic shock syndrome. In this study, we report the X-ray structure of the ternary complex between staphylococcal enterotoxin H (SEH) and its human receptors, MHC class II and TCR. The structure demonstrates that SEH predominantly interacts with the variable alpha-domain of TCR (TCRV alpha), which is supported by nuclear magnetic resonance (NMR) analyses. Furthermore, there is no contact between MHC and TCR upon complex... (More)
Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable beta-domain of TCR (TCRV beta). They induce a massive release of cytokines, which can lead to diseases such as food poisoning and toxic shock syndrome. In this study, we report the X-ray structure of the ternary complex between staphylococcal enterotoxin H (SEH) and its human receptors, MHC class II and TCR. The structure demonstrates that SEH predominantly interacts with the variable alpha-domain of TCR (TCRV alpha), which is supported by nuclear magnetic resonance (NMR) analyses. Furthermore, there is no contact between MHC and TCR upon complex formation. Structural analyses suggest that the major contact points to TCRV alpha are conserved among other bacterial SAgs. Consequently, a new dimension of SAg biology emerges, suggesting that in addition to the conventional interactions with the TCRV beta domain, SAgs can also activate T cells through the TCRV alpha domain. (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
Nature Communications
volume
1
publisher
Nature Publishing Group
external identifiers
  • wos:000288224800017
  • scopus:78650074574
ISSN
2041-1723
DOI
10.1038/ncomms1117
language
English
LU publication?
yes
id
c7a26ea4-0cda-4242-a9bd-9fb3b4a3ed0c (old id 1859416)
date added to LUP
2011-04-01 08:23:08
date last changed
2018-05-29 09:45:46
@article{c7a26ea4-0cda-4242-a9bd-9fb3b4a3ed0c,
  abstract     = {Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable beta-domain of TCR (TCRV beta). They induce a massive release of cytokines, which can lead to diseases such as food poisoning and toxic shock syndrome. In this study, we report the X-ray structure of the ternary complex between staphylococcal enterotoxin H (SEH) and its human receptors, MHC class II and TCR. The structure demonstrates that SEH predominantly interacts with the variable alpha-domain of TCR (TCRV alpha), which is supported by nuclear magnetic resonance (NMR) analyses. Furthermore, there is no contact between MHC and TCR upon complex formation. Structural analyses suggest that the major contact points to TCRV alpha are conserved among other bacterial SAgs. Consequently, a new dimension of SAg biology emerges, suggesting that in addition to the conventional interactions with the TCRV beta domain, SAgs can also activate T cells through the TCRV alpha domain.},
  articleno    = {119},
  author       = {Saline, Maria and Rodstrom, Karin E. J. and Fischer, Gerhard and Orekhov, Vladislav Yu. and Karlsson, B. Goran and Lindkvist, Karin},
  issn         = {2041-1723},
  language     = {eng},
  publisher    = {Nature Publishing Group},
  series       = {Nature Communications},
  title        = {The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation},
  url          = {http://dx.doi.org/10.1038/ncomms1117},
  volume       = {1},
  year         = {2010},
}