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The Journal of Immunology, 2007, 179: 2700-2704.
Copyright © 2007 by The American Association of Immunologists, Inc.

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Cutting Edge: Evidence of Direct TCR {alpha}-Chain Interaction with Superantigen1

Nick Pumphrey*, Annelise Vuidepot*, Bent Jakobsen*, Göran Forsberg{dagger}, Björn Walse{ddagger} and Karin Lindkvist-Petersson2,§

* Avidex Limited, Abingdon, Oxon, United Kingdom; {dagger} Active Biotech Research AB, Lund, Sweden; {ddagger} SARomics AB, Lund, Sweden; and § Department of Cell and Molecular Biology, Göteborg University, Göteborg, Sweden.

Superantigens are known to activate a large number of T cells. The SAg is presented by MHC class II on the APC and its classical feature is that it recognizes the variable region of the beta-chain of the TCR. In this article, we report, by direct binding studies, that staphylococcal enterotoxin (SE) H (SEH), a bacterial SAg secreted by Staphylococcus aureus, instead recognizes the variable {alpha}-chain (TRAV27) of TCR. Furthermore, we show that different SAgs (e.g., SEH and SEA) can simultaneously bind to one TCR by binding the {alpha}-chain and the beta-chain, respectively. Theoretical three-dimensional models of the penta complexes are presented. Hence, these findings open up a new dimension of the biology of the staphylococcal enterotoxins.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 This work was supported by the Swedish Foundation for Strategic Research and the Royal Swedish Academy of Sciences.

2 Address correspondence and reprint requests to Dr. Karin Lindkvist-Petersson, Department of Cell and Molecular Biology, Göteborg University, Box 462, S-405 30 Göteborg, Sweden. E-mail address: karin.lindkvist{at}gmm.gu.se

3 Abbreviations used in this paper: SAg, superantigen; RU, resonance unit; SE, staphylococcal enterotoxin; SPE-A, streptococcal pyrogenic exotoxin type A; TRAV, variable region of TCR {alpha}-chain; TRBV, variable region of TCR beta-chain.







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