SwePub - search: WFRF:(Skartved Niels Jörgen)

Enumeration	Reference	Cover	Find
1.	Lindkvist, Karin, et al. (author) Staphylococcal enterotoxin H induces V alpha-specific expansion of T cells. 2003 In: Journal of Immunology. - 1550-6606. ; 170:8, s. 4148-4154 Journal article (peer-reviewed)abstract Staphylococcal enterotoxin H (SEH) is a bacterial superantigen secreted by Staphylococcus aureus. Superantigens are presented on the MHC class II and activate large amounts of T cells by cross-linking APC and T cells. In this study, RT-PCR was used to show that SEH stimulates human T cells via the V domain of TCR, in particular V10 (TRAV27), while no TCR V-specific expansion was seen. This is in sharp contrast to all other studied bacterial superantigens, which are highly specific for TCR V. It was further confirmed by flow cytometry that SEH stimulation does not alter the levels of certain TCR V. In a functional assay addressing cross-reactivity, V binding superantigens were found to form one group, whereas SEH has different properties that fit well with V reactivity. As SEH binds on top of MHC class II, an interaction between MHC and TCR upon SEH binding is not likely. This concludes that the specific expansion of TCR V is not due to contacts between MHC and TCR, instead we suggest that SEH directly interacts with the TCR V domain.

Lindkvist, Karin, et al. (author)
Staphylococcal enterotoxin H induces V alpha-specific expansion of T cells.
2003
In: Journal of Immunology. - 1550-6606. ; 170:8, s. 4148-4154
Journal article (peer-reviewed)abstract
- Staphylococcal enterotoxin H (SEH) is a bacterial superantigen secreted by Staphylococcus aureus. Superantigens are presented on the MHC class II and activate large amounts of T cells by cross-linking APC and T cells. In this study, RT-PCR was used to show that SEH stimulates human T cells via the V domain of TCR, in particular V10 (TRAV27), while no TCR V-specific expansion was seen. This is in sharp contrast to all other studied bacterial superantigens, which are highly specific for TCR V. It was further confirmed by flow cytometry that SEH stimulation does not alter the levels of certain TCR V. In a functional assay addressing cross-reactivity, V binding superantigens were found to form one group, whereas SEH has different properties that fit well with V reactivity. As SEH binds on top of MHC class II, an interaction between MHC and TCR upon SEH binding is not likely. This concludes that the specific expansion of TCR V is not due to contacts between MHC and TCR, instead we suggest that SEH directly interacts with the TCR V domain.

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