Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain

Autores
Fernández, Marisa Mariel; Cho, Sangwoo; de Marzi, Mauricio Cesar; Kerzic, Melissa C.; Robinson, Howard; Mariuzza, Roy A.; Malchiodi, Emilio Luis
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR β chain (mVβ8.2) and staphylococcal enterotoxin G (SEG) at 2.0 Å resolution revealed a binding site that does not conserve the "hot spots" present in mVβ8.2-SEC2, mVβ8.2-SEC3, mVβ8.2-SEB, and mVβ8.2-SPEA complexes. Analysis of the mVβ8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mVβ8.2 by SEG. This mode of interaction between SEG and mVβ8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host.
Fil: Fernández, Marisa Mariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. University Of Maryland. Biotechnology Institute; Estados Unidos
Fil: Cho, Sangwoo. University Of Maryland. Biotechnology Institute; Estados Unidos
Fil: de Marzi, Mauricio Cesar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina
Fil: Kerzic, Melissa C.. University Of Maryland. Biotechnology Institute; Estados Unidos
Fil: Robinson, Howard. Brookhaven National Laboratory; Estados Unidos
Fil: Mariuzza, Roy A.. University Of Maryland. Biotechnology Institute; Estados Unidos
Fil: Malchiodi, Emilio Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. University Of Maryland. Biotechnology Institute; Estados Unidos
Materia
SUPERANTIGENS
T CELL RECEPTOR
CRYSTAL STRUCTURE
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:11336/217668
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chainFernández, Marisa MarielCho, Sangwoode Marzi, Mauricio CesarKerzic, Melissa C.Robinson, HowardMariuzza, Roy A.Malchiodi, Emilio LuisSUPERANTIGENST CELL RECEPTORCRYSTAL STRUCTUREhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR β chain (mVβ8.2) and staphylococcal enterotoxin G (SEG) at 2.0 Å resolution revealed a binding site that does not conserve the "hot spots" present in mVβ8.2-SEC2, mVβ8.2-SEC3, mVβ8.2-SEB, and mVβ8.2-SPEA complexes. Analysis of the mVβ8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mVβ8.2 by SEG. This mode of interaction between SEG and mVβ8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host.Fil: Fernández, Marisa Mariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. University Of Maryland. Biotechnology Institute; Estados UnidosFil: Cho, Sangwoo. University Of Maryland. Biotechnology Institute; Estados UnidosFil: de Marzi, Mauricio Cesar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. Universidad Nacional de Luján. Departamento de Ciencias Básicas; ArgentinaFil: Kerzic, Melissa C.. University Of Maryland. Biotechnology Institute; Estados UnidosFil: Robinson, Howard. Brookhaven National Laboratory; Estados UnidosFil: Mariuzza, Roy A.. University Of Maryland. Biotechnology Institute; Estados UnidosFil: Malchiodi, Emilio Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. University Of Maryland. Biotechnology Institute; Estados UnidosElsevier2011-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/217668Fernández, Marisa Mariel; Cho, Sangwoo; de Marzi, Mauricio Cesar; Kerzic, Melissa C.; Robinson, Howard; et al.; Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain; Elsevier; Journal of Biological Chemistry (online); 286; 2; 1-2011; 1189-11950021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0021925820563072info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M110.142471info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:55:45Zoai:ri.conicet.gov.ar:11336/217668instacron: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 09:55:46.08CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
title Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
spellingShingle Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
Fernández, Marisa Mariel
SUPERANTIGENS
T CELL RECEPTOR
CRYSTAL STRUCTURE
title_short Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
title_full Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
title_fullStr Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
title_full_unstemmed Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
title_sort Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain
dc.creator.none.fl_str_mv Fernández, Marisa Mariel
Cho, Sangwoo
de Marzi, Mauricio Cesar
Kerzic, Melissa C.
Robinson, Howard
Mariuzza, Roy A.
Malchiodi, Emilio Luis
author Fernández, Marisa Mariel
author_facet Fernández, Marisa Mariel
Cho, Sangwoo
de Marzi, Mauricio Cesar
Kerzic, Melissa C.
Robinson, Howard
Mariuzza, Roy A.
Malchiodi, Emilio Luis
author_role author
author2 Cho, Sangwoo
de Marzi, Mauricio Cesar
Kerzic, Melissa C.
Robinson, Howard
Mariuzza, Roy A.
Malchiodi, Emilio Luis
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv SUPERANTIGENS
T CELL RECEPTOR
CRYSTAL STRUCTURE
topic SUPERANTIGENS
T CELL RECEPTOR
CRYSTAL STRUCTURE
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) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR β chain (mVβ8.2) and staphylococcal enterotoxin G (SEG) at 2.0 Å resolution revealed a binding site that does not conserve the "hot spots" present in mVβ8.2-SEC2, mVβ8.2-SEC3, mVβ8.2-SEB, and mVβ8.2-SPEA complexes. Analysis of the mVβ8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mVβ8.2 by SEG. This mode of interaction between SEG and mVβ8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host.
Fil: Fernández, Marisa Mariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. University Of Maryland. Biotechnology Institute; Estados Unidos
Fil: Cho, Sangwoo. University Of Maryland. Biotechnology Institute; Estados Unidos
Fil: de Marzi, Mauricio Cesar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina
Fil: Kerzic, Melissa C.. University Of Maryland. Biotechnology Institute; Estados Unidos
Fil: Robinson, Howard. Brookhaven National Laboratory; Estados Unidos
Fil: Mariuzza, Roy A.. University Of Maryland. Biotechnology Institute; Estados Unidos
Fil: Malchiodi, Emilio Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina. University Of Maryland. Biotechnology Institute; Estados Unidos
description Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR β chain (mVβ8.2) and staphylococcal enterotoxin G (SEG) at 2.0 Å resolution revealed a binding site that does not conserve the "hot spots" present in mVβ8.2-SEC2, mVβ8.2-SEC3, mVβ8.2-SEB, and mVβ8.2-SPEA complexes. Analysis of the mVβ8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mVβ8.2 by SEG. This mode of interaction between SEG and mVβ8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host.
publishDate 2011
dc.date.none.fl_str_mv 2011-01
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/11336/217668
Fernández, Marisa Mariel; Cho, Sangwoo; de Marzi, Mauricio Cesar; Kerzic, Melissa C.; Robinson, Howard; et al.; Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain; Elsevier; Journal of Biological Chemistry (online); 286; 2; 1-2011; 1189-1195
0021-9258
CONICET Digital
CONICET
url http://hdl.handle.net/11336/217668
identifier_str_mv Fernández, Marisa Mariel; Cho, Sangwoo; de Marzi, Mauricio Cesar; Kerzic, Melissa C.; Robinson, Howard; et al.; Crystal structure of Staphylococcal Enterotoxin G (SEG) in complex with a mouse T-cell receptor β chain; Elsevier; Journal of Biological Chemistry (online); 286; 2; 1-2011; 1189-1195
0021-9258
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://www.sciencedirect.com/science/article/pii/S0021925820563072
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M110.142471
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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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