Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages

Autores
Herrera, Maria Georgina; Pizzuto, Malvina; Lonez, Caroline; Rott, Karsten; Hütten, Andreas; Sewald, Norbert; Ruysschaert, Jean-Marie; Dodero, Veronica Isabel
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Gliadin, an immunogenic protein present in wheat, is not fully degraded by humans and after the normal gastric and pancreatic digestion, the immunodominant 33-mer gliadin peptide remains unprocessed. The 33-mer gliadin peptide is found in human faeces and urine, proving not only its proteolytic resistance in vivo but more importantly its transport through the entire human body. Here, we demonstrate that 33-mer supramolecular structures larger than 220 nm induce the overexpression of nuclear factor kappa B (NF-κB) via a specific Toll-like Receptor (TLR) 2 and (TLR) 4 dependent pathway and the secretion of pro-inflammatory cytokines such as IP-10/CXCL10 and TNF-α. Using helium ion microscopy, we elucidated the initial stages of oligomerisation of 33-mer gliadin peptide, showing that rod-like oligomers are nucleation sites for protofilament formation. The relevance of the 33-mer supramolecular structures in the early stages of the disease is paving new perspectives in the understanding of gluten-related disorders.
Fil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
Fil: Pizzuto, Malvina. Université Libre de Bruxelles; Bélgica
Fil: Lonez, Caroline. Université Libre de Bruxelles; Bélgica
Fil: Rott, Karsten. Universitat Bielefeld; Alemania
Fil: Hütten, Andreas. Universitat Bielefeld; Alemania
Fil: Sewald, Norbert. Universitat Bielefeld; Alemania
Fil: Ruysschaert, Jean-Marie. Université Libre de Bruxelles; Bélgica
Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
Materia
CELIAC DISEASE
GLUTEN-RELATED DISORDERS
HELIUM ION MICROSCOPY
INNATE IMMUNE RESPONSE
OLIGOMERS
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:11336/93096
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/93096
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophagesHerrera, Maria GeorginaPizzuto, MalvinaLonez, CarolineRott, KarstenHütten, AndreasSewald, NorbertRuysschaert, Jean-MarieDodero, Veronica IsabelCELIAC DISEASEGLUTEN-RELATED DISORDERSHELIUM ION MICROSCOPYINNATE IMMUNE RESPONSEOLIGOMERShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Gliadin, an immunogenic protein present in wheat, is not fully degraded by humans and after the normal gastric and pancreatic digestion, the immunodominant 33-mer gliadin peptide remains unprocessed. The 33-mer gliadin peptide is found in human faeces and urine, proving not only its proteolytic resistance in vivo but more importantly its transport through the entire human body. Here, we demonstrate that 33-mer supramolecular structures larger than 220 nm induce the overexpression of nuclear factor kappa B (NF-κB) via a specific Toll-like Receptor (TLR) 2 and (TLR) 4 dependent pathway and the secretion of pro-inflammatory cytokines such as IP-10/CXCL10 and TNF-α. Using helium ion microscopy, we elucidated the initial stages of oligomerisation of 33-mer gliadin peptide, showing that rod-like oligomers are nucleation sites for protofilament formation. The relevance of the 33-mer supramolecular structures in the early stages of the disease is paving new perspectives in the understanding of gluten-related disorders.Fil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; AlemaniaFil: Pizzuto, Malvina. Université Libre de Bruxelles; BélgicaFil: Lonez, Caroline. Université Libre de Bruxelles; BélgicaFil: Rott, Karsten. Universitat Bielefeld; AlemaniaFil: Hütten, Andreas. Universitat Bielefeld; AlemaniaFil: Sewald, Norbert. Universitat Bielefeld; AlemaniaFil: Ruysschaert, Jean-Marie. Université Libre de Bruxelles; BélgicaFil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; AlemaniaElsevier Science2018-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/93096Herrera, Maria Georgina; Pizzuto, Malvina; Lonez, Caroline; Rott, Karsten; Hütten, Andreas; et al.; Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages; Elsevier Science; Nanomedicine-nanotechnology Biology And Medicine; 14; 4; 6-2018; 1417-14271549-9634CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S1549963418300868info:eu-repo/semantics/altIdentifier/doi/10.1016/j.nano.2018.04.014info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:40:27Zoai:ri.conicet.gov.ar:11336/93096instacron: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:34982025-09-29 10:40:28.064CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
title Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
spellingShingle Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
Herrera, Maria Georgina
CELIAC DISEASE
GLUTEN-RELATED DISORDERS
HELIUM ION MICROSCOPY
INNATE IMMUNE RESPONSE
OLIGOMERS
title_short Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
title_full Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
title_fullStr Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
title_full_unstemmed Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
title_sort Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
dc.creator.none.fl_str_mv Herrera, Maria Georgina
Pizzuto, Malvina
Lonez, Caroline
Rott, Karsten
Hütten, Andreas
Sewald, Norbert
Ruysschaert, Jean-Marie
Dodero, Veronica Isabel
author Herrera, Maria Georgina
author_facet Herrera, Maria Georgina
Pizzuto, Malvina
Lonez, Caroline
Rott, Karsten
Hütten, Andreas
Sewald, Norbert
Ruysschaert, Jean-Marie
Dodero, Veronica Isabel
author_role author
author2 Pizzuto, Malvina
Lonez, Caroline
Rott, Karsten
Hütten, Andreas
Sewald, Norbert
Ruysschaert, Jean-Marie
Dodero, Veronica Isabel
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CELIAC DISEASE
GLUTEN-RELATED DISORDERS
HELIUM ION MICROSCOPY
INNATE IMMUNE RESPONSE
OLIGOMERS
topic CELIAC DISEASE
GLUTEN-RELATED DISORDERS
HELIUM ION MICROSCOPY
INNATE IMMUNE RESPONSE
OLIGOMERS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Gliadin, an immunogenic protein present in wheat, is not fully degraded by humans and after the normal gastric and pancreatic digestion, the immunodominant 33-mer gliadin peptide remains unprocessed. The 33-mer gliadin peptide is found in human faeces and urine, proving not only its proteolytic resistance in vivo but more importantly its transport through the entire human body. Here, we demonstrate that 33-mer supramolecular structures larger than 220 nm induce the overexpression of nuclear factor kappa B (NF-κB) via a specific Toll-like Receptor (TLR) 2 and (TLR) 4 dependent pathway and the secretion of pro-inflammatory cytokines such as IP-10/CXCL10 and TNF-α. Using helium ion microscopy, we elucidated the initial stages of oligomerisation of 33-mer gliadin peptide, showing that rod-like oligomers are nucleation sites for protofilament formation. The relevance of the 33-mer supramolecular structures in the early stages of the disease is paving new perspectives in the understanding of gluten-related disorders.
Fil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
Fil: Pizzuto, Malvina. Université Libre de Bruxelles; Bélgica
Fil: Lonez, Caroline. Université Libre de Bruxelles; Bélgica
Fil: Rott, Karsten. Universitat Bielefeld; Alemania
Fil: Hütten, Andreas. Universitat Bielefeld; Alemania
Fil: Sewald, Norbert. Universitat Bielefeld; Alemania
Fil: Ruysschaert, Jean-Marie. Université Libre de Bruxelles; Bélgica
Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
description Gliadin, an immunogenic protein present in wheat, is not fully degraded by humans and after the normal gastric and pancreatic digestion, the immunodominant 33-mer gliadin peptide remains unprocessed. The 33-mer gliadin peptide is found in human faeces and urine, proving not only its proteolytic resistance in vivo but more importantly its transport through the entire human body. Here, we demonstrate that 33-mer supramolecular structures larger than 220 nm induce the overexpression of nuclear factor kappa B (NF-κB) via a specific Toll-like Receptor (TLR) 2 and (TLR) 4 dependent pathway and the secretion of pro-inflammatory cytokines such as IP-10/CXCL10 and TNF-α. Using helium ion microscopy, we elucidated the initial stages of oligomerisation of 33-mer gliadin peptide, showing that rod-like oligomers are nucleation sites for protofilament formation. The relevance of the 33-mer supramolecular structures in the early stages of the disease is paving new perspectives in the understanding of gluten-related disorders.
publishDate 2018
dc.date.none.fl_str_mv 2018-06
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/11336/93096
Herrera, Maria Georgina; Pizzuto, Malvina; Lonez, Caroline; Rott, Karsten; Hütten, Andreas; et al.; Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages; Elsevier Science; Nanomedicine-nanotechnology Biology And Medicine; 14; 4; 6-2018; 1417-1427
1549-9634
CONICET Digital
CONICET
url http://hdl.handle.net/11336/93096
identifier_str_mv Herrera, Maria Georgina; Pizzuto, Malvina; Lonez, Caroline; Rott, Karsten; Hütten, Andreas; et al.; Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages; Elsevier Science; Nanomedicine-nanotechnology Biology And Medicine; 14; 4; 6-2018; 1417-1427
1549-9634
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S1549963418300868
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.nano.2018.04.014
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 Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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
_version_ 1844614432894746624
score 13.070432

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