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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/47707

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network_name_str CONICET Digital (CONICET)
spelling 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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