Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition

T cells are crucial players in cell-mediated immunity. The specificity of their receptor, the T cell receptor (TCR), is central for the immune system to distinguish foreign from host antigens. Superantigens are bacterial toxins capable of inducing a toxic immune response by cross-linking the TCR and...

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Bibliographic Details
Published in:PloS one 2015-07, Vol.10 (7), p.e0131988
Main Authors: Rödström, Karin E J, Regenthal, Paulina, Lindkvist-Petersson, Karin
Format: Article
Language:English
Subjects:
Antigens
Bacteria
Basic Medicine
Bioinformatics
Cell-mediated immunity
Chains
Chromatography
Complex formation
Crosslinking
Crystal structure
Crystallography, X-Ray
Enterotoxins - metabolism
Glycerol
Humans
Immune response
Immune system
Immunity
Immunity, Cellular - immunology
Immunologi inom det medicinska området
Immunology
Immunology in the medical area
Lymphocytes
Lymphocytes T
Major histocompatibility complex
Medical and Health Sciences
Medicin och hälsovetenskap
Medicinska och farmaceutiska grundvetenskaper
Peptides
Protein Conformation
Proteins
Receptors, Antigen, T-Cell - metabolism
Staphylococcal enterotoxin E
Staphylococcus aureus - immunology
Superantigens
Superantigens - metabolism
T cell receptors
T cells
T-cell receptor
Toxins
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Summary:T cells are crucial players in cell-mediated immunity. The specificity of their receptor, the T cell receptor (TCR), is central for the immune system to distinguish foreign from host antigens. Superantigens are bacterial toxins capable of inducing a toxic immune response by cross-linking the TCR and the major histocompatibility complex (MHC) class II and circumventing the antigen specificity. Here, we present the structure of staphylococcal enterotoxin E (SEE) in complex with a human T cell receptor, as well as the unligated T cell receptor structure. There are clear structural changes in the TCR loops upon superantigen binding. In particular, the HV4 loop moves to circumvent steric clashes upon complex formation. In addition, a predicted ternary model of SEE in complex with both TCR and MHC class II displays intermolecular contacts between the TCR α-chain and the MHC, suggesting that the TCR α-chain is of importance for complex formation.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0131988