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The structure of su...
The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation.
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- Saline, Maria (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Svenskt NMR-centrum vid Göteborgs universitet,Department of Chemistry,Swedish NMR Centre at Göteborg University
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- Rödström, Karin, 1986 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för cell- och molekylärbiologi,Svenskt NMR-centrum vid Göteborgs universitet,Department of Cell and Molecular Biology,Swedish NMR Centre at Göteborg University
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- Fischer, Gerhard, 1978 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry
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- Orekhov, Vladislav, 1966 (author)
- Gothenburg University,Göteborgs universitet,Svenskt NMR-centrum vid Göteborgs universitet,Institutionen för kemi,Swedish NMR Centre at Göteborg University,Department of Chemistry
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- Karlsson, B Göran, 1962 (author)
- Gothenburg University,Göteborgs universitet,Svenskt NMR-centrum vid Göteborgs universitet,Swedish NMR Centre at Göteborg University
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- Lindkvist-Petersson, Karin (author)
- Lund University,Lunds universitet,Gothenburg University,Göteborgs universitet,Institutionen för cell- och molekylärbiologi,Department of Cell and Molecular Biology,Institutionen för experimentell medicinsk vetenskap,Medicinska fakulteten,Department of Experimental Medical Science,Faculty of Medicine
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(creator_code:org_t)
- 2010-11-16
- 2010
- English.
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In: Nature communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 1:8
- Related links:
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http://dx.doi.org/10...
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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Abstract
Subject headings
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- Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable β-domain of TCR (TCRVβ). 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 α-domain of TCR (TCRVα), 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 TCRVα are conserved among other bacterial SAgs. Consequently, a new dimension of SAg biology emerges, suggesting that in addition to the conventional interactions with the TCRVβ domain, SAgs can also activate T cells through the TCRVα domain.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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