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Structural studies of staphylococcal enterotoxin H in complex with T cell receptor and major histocompatibility complex class II

Poster (konferens)
Författare Karin Rödström
Maria Saline
Gerhard Fischer
Karin Lindkvist-Petersson
Publicerad i FEBS JOURNAL
Volym 2010, 277
Sidor 53-54
ISSN 1742-464X
Publiceringsår 2010
Publicerad vid Institutionen för cell- och molekylärbiologi
Institutionen för kemi
Svenskt NMR-centrum vid Göteborgs universitet
Sidor 53-54
Språk en
Ämneskategorier Strukturbiologi, Immunologi

Sammanfattning

Superantigens (SAgs) are bacterial toxins capable of cross-linking the immune receptors of the host, the T cell receptor (TCR) and major histocompatibility complex (MHC) class II, and thereby trigger a massive release of cytokines. This could lead to toxic shock syndrome, which can have a fatal outcome. Here, we present the crystal structure of the ternary complex between the superantigen, staphylococcal enterotoxin H (SEH), TCR and MHC, as well as the dimer complex, including only TCR and SEH. It is evident that SEH interacts with the variable α domain (Vα) of TCR, in sharp contrast to previously studied SAgs that interact with the Vβ domain. Due to the high structural conservation of amino acids in SEH that are crucial for the interaction, we propose that in addition to Vβ activation of T cells, there are SAgs, in addition to SEH, which are able to activate T cells through Vα as well. In addition to providing crucial information regarding the nature of TCR-mediated recognition of superantigens, the finding have central implications for future strategies aimed at preventing or modulating the often pathogenic response to superantigens.

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