Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.
(2015) In PLoS ONE 10(7).- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/7746845
- author
- Rödström, Karin LU ; Regenthal, Paulina LU and Lindkvist, Karin LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- PLoS ONE
- volume
- 10
- issue
- 7
- article number
- e0131988
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- pmid:26147596
- wos:000358157600175
- scopus:84940069363
- pmid:26147596
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0131988
- language
- English
- LU publication?
- yes
- id
- b76065a5-e71a-421a-a2d0-484017e1b14a (old id 7746845)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/26147596?dopt=Abstract
- date added to LUP
- 2016-04-01 14:17:20
- date last changed
- 2022-04-06 17:44:37
@article{b76065a5-e71a-421a-a2d0-484017e1b14a, abstract = {{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.}}, author = {{Rödström, Karin and Regenthal, Paulina and Lindkvist, Karin}}, issn = {{1932-6203}}, language = {{eng}}, number = {{7}}, publisher = {{Public Library of Science (PLoS)}}, series = {{PLoS ONE}}, title = {{Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.}}, url = {{http://dx.doi.org/10.1371/journal.pone.0131988}}, doi = {{10.1371/journal.pone.0131988}}, volume = {{10}}, year = {{2015}}, }