Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes
- Autores
- Sundberg, Eric J.; Li, Hongmin; Llera, Andrea Sabina; McCormick, John K.; Tormo, José; Schlievert, Patrick M.; Karjalainen, Klaus; Mariuzza, Roy A.
- Año de publicación
- 2002
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR beta chain ligands that reveal distinct TCR binding modes. The SpeC-TCR beta chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation.
Fil: Sundberg, Eric J.. University of Maryland; Estados Unidos
Fil: Li, Hongmin. University of Maryland; Estados Unidos
Fil: Llera, Andrea Sabina. University of Maryland; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: McCormick, John K.. University of Minnesota; Estados Unidos
Fil: Tormo, José. University of Maryland; Estados Unidos. Universidad Autónoma de Madrid; España
Fil: Schlievert, Patrick M.. University of Minnesota; Estados Unidos
Fil: Karjalainen, Klaus. Basel Institute for Immunology; Suiza
Fil: Mariuzza, Roy A.. University of Maryland; Estados Unidos - Materia
-
Superantigen
T Cell Receptor - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/47707
Ver los metadatos del registro completo
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Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling ComplexesSundberg, Eric J.Li, HongminLlera, Andrea SabinaMcCormick, John K.Tormo, JoséSchlievert, Patrick M.Karjalainen, KlausMariuzza, Roy A.SuperantigenT Cell Receptorhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR beta chain ligands that reveal distinct TCR binding modes. The SpeC-TCR beta chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation.Fil: Sundberg, Eric J.. University of Maryland; Estados UnidosFil: Li, Hongmin. University of Maryland; Estados UnidosFil: Llera, Andrea Sabina. University of Maryland; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: McCormick, John K.. University of Minnesota; Estados UnidosFil: Tormo, José. University of Maryland; Estados Unidos. Universidad Autónoma de Madrid; EspañaFil: Schlievert, Patrick M.. University of Minnesota; Estados UnidosFil: Karjalainen, Klaus. Basel Institute for Immunology; SuizaFil: Mariuzza, Roy A.. University of Maryland; Estados UnidosCell Press2002-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/47707Sundberg, Eric J.; Li, Hongmin; Llera, Andrea Sabina; McCormick, John K.; Tormo, José; et al.; Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes; Cell Press; Structure With Folding & Design.; 10; 5; 5-2002; 687-6990969-21261878-4186CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0969212602007591info:eu-repo/semantics/altIdentifier/doi/10.1016/S0969-2126(02)00759-1info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:08:19Zoai:ri.conicet.gov.ar:11336/47707instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:08:20.191CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes |
title |
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes |
spellingShingle |
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes Sundberg, Eric J. Superantigen T Cell Receptor |
title_short |
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes |
title_full |
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes |
title_fullStr |
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes |
title_full_unstemmed |
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes |
title_sort |
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes |
dc.creator.none.fl_str_mv |
Sundberg, Eric J. Li, Hongmin Llera, Andrea Sabina McCormick, John K. Tormo, José Schlievert, Patrick M. Karjalainen, Klaus Mariuzza, Roy A. |
author |
Sundberg, Eric J. |
author_facet |
Sundberg, Eric J. Li, Hongmin Llera, Andrea Sabina McCormick, John K. Tormo, José Schlievert, Patrick M. Karjalainen, Klaus Mariuzza, Roy A. |
author_role |
author |
author2 |
Li, Hongmin Llera, Andrea Sabina McCormick, John K. Tormo, José Schlievert, Patrick M. Karjalainen, Klaus Mariuzza, Roy A. |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Superantigen T Cell Receptor |
topic |
Superantigen T Cell Receptor |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR beta chain ligands that reveal distinct TCR binding modes. The SpeC-TCR beta chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation. Fil: Sundberg, Eric J.. University of Maryland; Estados Unidos Fil: Li, Hongmin. University of Maryland; Estados Unidos Fil: Llera, Andrea Sabina. University of Maryland; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: McCormick, John K.. University of Minnesota; Estados Unidos Fil: Tormo, José. University of Maryland; Estados Unidos. Universidad Autónoma de Madrid; España Fil: Schlievert, Patrick M.. University of Minnesota; Estados Unidos Fil: Karjalainen, Klaus. Basel Institute for Immunology; Suiza Fil: Mariuzza, Roy A.. University of Maryland; Estados Unidos |
description |
Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR beta chain ligands that reveal distinct TCR binding modes. The SpeC-TCR beta chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002-05 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/47707 Sundberg, Eric J.; Li, Hongmin; Llera, Andrea Sabina; McCormick, John K.; Tormo, José; et al.; Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes; Cell Press; Structure With Folding & Design.; 10; 5; 5-2002; 687-699 0969-2126 1878-4186 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/47707 |
identifier_str_mv |
Sundberg, Eric J.; Li, Hongmin; Llera, Andrea Sabina; McCormick, John K.; Tormo, José; et al.; Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes; Cell Press; Structure With Folding & Design.; 10; 5; 5-2002; 687-699 0969-2126 1878-4186 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0969212602007591 info:eu-repo/semantics/altIdentifier/doi/10.1016/S0969-2126(02)00759-1 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Cell Press |
publisher.none.fl_str_mv |
Cell Press |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1842270040587501568 |
score |
13.13397 |