The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model

Autores
Herrera, Maria Georgina; Amundarain, María Julia; Dörfler, Philipp W.; Dodero, Veronica Isabel
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Celiac disease (CeD) is an autoimmune disorder triggered by gluten proteins, affecting approximately 1 % of the global population. The 33-mer deamidated gliadin peptide (DGP) is a metabolically modified wheat-gluten superantigen for CeD. Here, we demonstrate that the 33-mer DGP spontaneously assembles into oligomers with a diameter of approximately 24 nm. The 33-mer DGP oligomers present two main secondary structural motifs?a major polyproline II helix and a minor β-sheet structure. Importantly, in the presence of 33-mer DGP oligomers, there is a statistically significant increase in the permeability in the gut epithelial cell model Caco-2, accompanied by the redistribution of zonula occludens-1, a master tight junction protein. These findings provide novel molecular and supramolecular insights into the impact of 33-mer DGP in CeD and highlight the relevance of gliadin peptide oligomerization.
Fil: Herrera, Maria Georgina. Ruhr Universität Bochum; Alemania. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biociencias, Biotecnología y Biología Traslacional; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biociencias, Biotecnología y Biología Traslacional.; Argentina
Fil: Dörfler, Philipp W.. Universitat Bielefeld; Alemania
Fil: Dodero, Veronica Isabel. Universitat Bielefeld; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
POLYPROLINE II
CELIAC DISEASE
OLIGOMERIZATION
PEPTIDES
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:11336/260350
Acceder
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network_name_str CONICET Digital (CONICET)
spelling The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell ModelHerrera, Maria GeorginaAmundarain, María JuliaDörfler, Philipp W.Dodero, Veronica IsabelPOLYPROLINE IICELIAC DISEASEOLIGOMERIZATIONPEPTIDEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Celiac disease (CeD) is an autoimmune disorder triggered by gluten proteins, affecting approximately 1 % of the global population. The 33-mer deamidated gliadin peptide (DGP) is a metabolically modified wheat-gluten superantigen for CeD. Here, we demonstrate that the 33-mer DGP spontaneously assembles into oligomers with a diameter of approximately 24 nm. The 33-mer DGP oligomers present two main secondary structural motifs?a major polyproline II helix and a minor β-sheet structure. Importantly, in the presence of 33-mer DGP oligomers, there is a statistically significant increase in the permeability in the gut epithelial cell model Caco-2, accompanied by the redistribution of zonula occludens-1, a master tight junction protein. These findings provide novel molecular and supramolecular insights into the impact of 33-mer DGP in CeD and highlight the relevance of gliadin peptide oligomerization.Fil: Herrera, Maria Georgina. Ruhr Universität Bochum; Alemania. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biociencias, Biotecnología y Biología Traslacional; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biociencias, Biotecnología y Biología Traslacional.; ArgentinaFil: Dörfler, Philipp W.. Universitat Bielefeld; AlemaniaFil: Dodero, Veronica Isabel. Universitat Bielefeld; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaWiley VCH Verlag2024-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/260350Herrera, Maria Georgina; Amundarain, María Julia; Dörfler, Philipp W.; Dodero, Veronica Isabel; The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model; Wiley VCH Verlag; Angewandte Chemie; 63; 21; 4-2024; 1-71433-7851CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1002/anie.202317552info:eu-repo/semantics/altIdentifier/doi/10.1002/anie.202317552info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:06:09Zoai:ri.conicet.gov.ar:11336/260350instacron: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:34982025-10-15 15:06:10.007CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model
title The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model
spellingShingle The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model
Herrera, Maria Georgina
POLYPROLINE II
CELIAC DISEASE
OLIGOMERIZATION
PEPTIDES
title_short The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model
title_full The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model
title_fullStr The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model
title_full_unstemmed The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model
title_sort The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model
dc.creator.none.fl_str_mv Herrera, Maria Georgina
Amundarain, María Julia
Dörfler, Philipp W.
Dodero, Veronica Isabel
author Herrera, Maria Georgina
author_facet Herrera, Maria Georgina
Amundarain, María Julia
Dörfler, Philipp W.
Dodero, Veronica Isabel
author_role author
author2 Amundarain, María Julia
Dörfler, Philipp W.
Dodero, Veronica Isabel
author2_role author
author
author
dc.subject.none.fl_str_mv POLYPROLINE II
CELIAC DISEASE
OLIGOMERIZATION
PEPTIDES
topic POLYPROLINE II
CELIAC DISEASE
OLIGOMERIZATION
PEPTIDES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Celiac disease (CeD) is an autoimmune disorder triggered by gluten proteins, affecting approximately 1 % of the global population. The 33-mer deamidated gliadin peptide (DGP) is a metabolically modified wheat-gluten superantigen for CeD. Here, we demonstrate that the 33-mer DGP spontaneously assembles into oligomers with a diameter of approximately 24 nm. The 33-mer DGP oligomers present two main secondary structural motifs?a major polyproline II helix and a minor β-sheet structure. Importantly, in the presence of 33-mer DGP oligomers, there is a statistically significant increase in the permeability in the gut epithelial cell model Caco-2, accompanied by the redistribution of zonula occludens-1, a master tight junction protein. These findings provide novel molecular and supramolecular insights into the impact of 33-mer DGP in CeD and highlight the relevance of gliadin peptide oligomerization.
Fil: Herrera, Maria Georgina. Ruhr Universität Bochum; Alemania. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biociencias, Biotecnología y Biología Traslacional; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Amundarain, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biociencias, Biotecnología y Biología Traslacional.; Argentina
Fil: Dörfler, Philipp W.. Universitat Bielefeld; Alemania
Fil: Dodero, Veronica Isabel. Universitat Bielefeld; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Celiac disease (CeD) is an autoimmune disorder triggered by gluten proteins, affecting approximately 1 % of the global population. The 33-mer deamidated gliadin peptide (DGP) is a metabolically modified wheat-gluten superantigen for CeD. Here, we demonstrate that the 33-mer DGP spontaneously assembles into oligomers with a diameter of approximately 24 nm. The 33-mer DGP oligomers present two main secondary structural motifs?a major polyproline II helix and a minor β-sheet structure. Importantly, in the presence of 33-mer DGP oligomers, there is a statistically significant increase in the permeability in the gut epithelial cell model Caco-2, accompanied by the redistribution of zonula occludens-1, a master tight junction protein. These findings provide novel molecular and supramolecular insights into the impact of 33-mer DGP in CeD and highlight the relevance of gliadin peptide oligomerization.
publishDate 2024
dc.date.none.fl_str_mv 2024-04
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/11336/260350
Herrera, Maria Georgina; Amundarain, María Julia; Dörfler, Philipp W.; Dodero, Veronica Isabel; The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model; Wiley VCH Verlag; Angewandte Chemie; 63; 21; 4-2024; 1-7
1433-7851
CONICET Digital
CONICET
url http://hdl.handle.net/11336/260350
identifier_str_mv Herrera, Maria Georgina; Amundarain, María Julia; Dörfler, Philipp W.; Dodero, Veronica Isabel; The Celiac‐Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model; Wiley VCH Verlag; Angewandte Chemie; 63; 21; 4-2024; 1-7
1433-7851
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://onlinelibrary.wiley.com/doi/10.1002/anie.202317552
info:eu-repo/semantics/altIdentifier/doi/10.1002/anie.202317552
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
application/pdf
dc.publisher.none.fl_str_mv Wiley VCH Verlag
publisher.none.fl_str_mv Wiley VCH Verlag
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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score 12.891075

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