Superantigens interact with MHC class II molecules outside of the antigen groove

Dellabona, Paolo; Peccoud, Jean; Kappler, John W.; Marrack, Philippa; Benoist, Christophe; Mathis, Diane

doi:10.1016/0092-8674(90)90388-u

Cited by 410 publications

(227 citation statements)

References 46 publications

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“…Mast cells could also participate in the first step of the immune response, since it was elegantly demonstrated that rodent mast cells express major histocompatibility complex (MHC) class II molecules [29][30][31][32][33][34] and have the capacity to process nominal antigens and present immunogenic peptides to T cells [31,35,36]. The possible involvement of signaling via MHC class II molecules in specific immunological processes is further reinforced by the observation that, in some primates, connective tissue mast cells were detected undergoing degranulation after intradermal injection of staphylococcal enterotoxin B (SEB) [37][38][39], a natural ligand of MHC class II molecules that does not require processing by antigen-presenting cells in order to activate T cells [40].…”

Section: Introductionmentioning

confidence: 99%

Expression of functional major histocompatility complex class II molecules on HMC-1 human mast cells

Dimitriadou

Mécheri

Koutsilieris

et al. 1998

Journal of Leukocyte Biology

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Section: Introductionmentioning

confidence: 99%

Expression of functional major histocompatility complex class II molecules on HMC-1 human mast cells

Dimitriadou

Mécheri

Koutsilieris

et al. 1998

Journal of Leukocyte Biology

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“…These superantigens bind as unprocessed proteins outside the peptide-binding groove of MHC class II (14) to two completely distinct binding sites. Site-directed mutagenesis studies (15)(16)(17)(18) and structural studies of SEA D227A -HLA-DR1 (19) and SEB-HLA-DR1 complexes (20) show that SEA, SEB, SEC, SED, and SEE bind to the ␣-chain of MHC class II with low affinity using its N-terminal domain.…”

mentioning

confidence: 99%

Staphylococcal Enterotoxin H Induces Vα-Specific Expansion of T Cells

Petersson

Pettersson

Skartved

et al. 2003

The Journal of Immunology

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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 Vα domain of TCR, in particular Vα10 (TRAV27), while no TCR Vβ-specific expansion was seen. This is in sharp contrast to all other studied bacterial superantigens, which are highly specific for TCR Vβ. It was further confirmed by flow cytometry that SEH stimulation does not alter the levels of certain TCR Vβ. In a functional assay addressing cross-reactivity, Vβ binding superantigens were found to form one group, whereas SEH has different properties that fit well with Vα 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 Vα is not due to contacts between MHC and TCR, instead we suggest that SEH directly interacts with the TCR Vα domain.

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“…This factor, the molecular characteristics of which have not been fully defined, has been termed M urthritidis mitogen (MAM) and recently classified as a superantigen (1 1,12). The term superantigen was coined to denote molecules that need not be processed (13)(14)(15)(16), bind outside the classical peptide-binding groove of class I1 major histocompatibility complex (MHC) molecules (17,18) and stimulate almost entire sets of T cells expressing specific T cell receptor V, gene products (19). A variety of bacterial and viral products have been documented to act as superantigens (for review, see refs.…”

mentioning

confidence: 99%

Mycoplasma arthritidis mitogen. V_β engaged in mice, rats, and humans, and requirement of HLA‐DRα for presentation

Baccalà

Smith

Vestberg

et al. 1992

Arthritis & Rheumatism

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Objective. Mycoplasma arthritidis mitogen (MAM) is mitogenic for mouse, rat, and human T cells, and behaves as a superantigen in mice through its capacity to bind to the (Y chain of I-E molecules and engage entire sets of T cells expressing specific Vp. Here, we have attempted to fully characterize the V,-engaging activities of MAM in mice, and define similar activities in rats and humans.Methods. Multiprobe RNase-protection assays and mice transgenic for human DRcu, DRP, and DRaP were utilized for this purpose.Results. MAM-reactive V ' in the mouse included not only the previously reported V&, Vp8.1, Vp8.2, and V9.3, but also V,5.1. In the rat, engagement of Vs.1, V&, V9.1, and V'8.2, but not Vp8.3, was documented, whereas in humans, the engaged V , included primarily V,19.1 (alternatively termed V'17.1) and, to a lesser ~.. Publication No. 7007-1MM from the

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Superantigens interact with MHC class II molecules outside of the antigen groove

Cited by 410 publications

References 46 publications

Expression of functional major histocompatility complex class II molecules on HMC-1 human mast cells

Expression of functional major histocompatility complex class II molecules on HMC-1 human mast cells

Staphylococcal Enterotoxin H Induces Vα-Specific Expansion of T Cells

Mycoplasma arthritidis mitogen. V_β engaged in mice, rats, and humans, and requirement of HLA‐DRα for presentation

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Superantigens interact with MHC class II molecules outside of the antigen groove

Cited by 410 publications

References 46 publications

Expression of functional major histocompatility complex class II molecules on HMC-1 human mast cells

Expression of functional major histocompatility complex class II molecules on HMC-1 human mast cells

Staphylococcal Enterotoxin H Induces Vα-Specific Expansion of T Cells

Mycoplasma arthritidis mitogen. Vβ engaged in mice, rats, and humans, and requirement of HLA‐DRα for presentation

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Mycoplasma arthritidis mitogen. V_β engaged in mice, rats, and humans, and requirement of HLA‐DRα for presentation