The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

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

På svenska

Author

  • Maria Saline
  • Karin E. J. Rodstrom
  • Gerhard Fischer
  • Vladislav Yu. Orekhov
  • B. Goran Karlsson
  • Karin Lindkvist

Summary, in English

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.

Publishing year

2010

Language

English

Publication/Series

Nature Communications

Volume

1

Document type

Journal article

Publisher

Nature Publishing Group

Topic

  • Basic Medicine

Status

Published

ISBN/ISSN/Other

  • ISSN: 2041-1723