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Lipopolysaccharides with Acylation Defects Potentiate TLR4 Signaling and Shape T Cell Responses
Lipopolysaccharides or endotoxins are components of Gram-negative enterobacteria that cause septic shock in mammals. However, a LPS carrying hexa-acyl lipid A moieties is highly endotoxic compared to a tetra-acyl LPS and the latter has been considered as an antagonist of hexa-acyl LPS-mediated TLR4...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3563657/ https://www.ncbi.nlm.nih.gov/pubmed/23390517 http://dx.doi.org/10.1371/journal.pone.0055117 |
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author | Martirosyan, Anna Ohne, Yoichiro Degos, Clara Gorvel, Laurent Moriyón, Ignacio Oh, Sangkon Gorvel, Jean-Pierre |
author_facet | Martirosyan, Anna Ohne, Yoichiro Degos, Clara Gorvel, Laurent Moriyón, Ignacio Oh, Sangkon Gorvel, Jean-Pierre |
author_sort | Martirosyan, Anna |
collection | PubMed |
description | Lipopolysaccharides or endotoxins are components of Gram-negative enterobacteria that cause septic shock in mammals. However, a LPS carrying hexa-acyl lipid A moieties is highly endotoxic compared to a tetra-acyl LPS and the latter has been considered as an antagonist of hexa-acyl LPS-mediated TLR4 signaling. We investigated the relationship between the structure and the function of bacterial LPS in the context of human and mouse dendritic cell activation. Strikingly, LPS with acylation defects were capable of triggering a strong and early TLR4-dependent DC activation, which in turn led to the activation of the proteasome machinery dampening the pro-inflammatory cytokine secretion. Upon activation with tetra-acyl LPS both mouse and human dendritic cells triggered CD4(+) T and CD8(+) T cell responses and, importantly, human myeloid dendritic cells favored the induction of regulatory T cells. Altogether, our data suggest that LPS acylation controlled by pathogenic bacteria might be an important strategy to subvert adaptive immunity. |
format | Online Article Text |
id | pubmed-3563657 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-35636572013-02-06 Lipopolysaccharides with Acylation Defects Potentiate TLR4 Signaling and Shape T Cell Responses Martirosyan, Anna Ohne, Yoichiro Degos, Clara Gorvel, Laurent Moriyón, Ignacio Oh, Sangkon Gorvel, Jean-Pierre PLoS One Research Article Lipopolysaccharides or endotoxins are components of Gram-negative enterobacteria that cause septic shock in mammals. However, a LPS carrying hexa-acyl lipid A moieties is highly endotoxic compared to a tetra-acyl LPS and the latter has been considered as an antagonist of hexa-acyl LPS-mediated TLR4 signaling. We investigated the relationship between the structure and the function of bacterial LPS in the context of human and mouse dendritic cell activation. Strikingly, LPS with acylation defects were capable of triggering a strong and early TLR4-dependent DC activation, which in turn led to the activation of the proteasome machinery dampening the pro-inflammatory cytokine secretion. Upon activation with tetra-acyl LPS both mouse and human dendritic cells triggered CD4(+) T and CD8(+) T cell responses and, importantly, human myeloid dendritic cells favored the induction of regulatory T cells. Altogether, our data suggest that LPS acylation controlled by pathogenic bacteria might be an important strategy to subvert adaptive immunity. Public Library of Science 2013-02-04 /pmc/articles/PMC3563657/ /pubmed/23390517 http://dx.doi.org/10.1371/journal.pone.0055117 Text en © 2013 Martirosyan et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Martirosyan, Anna Ohne, Yoichiro Degos, Clara Gorvel, Laurent Moriyón, Ignacio Oh, Sangkon Gorvel, Jean-Pierre Lipopolysaccharides with Acylation Defects Potentiate TLR4 Signaling and Shape T Cell Responses |
title | Lipopolysaccharides with Acylation Defects Potentiate TLR4 Signaling and Shape T Cell Responses |
title_full | Lipopolysaccharides with Acylation Defects Potentiate TLR4 Signaling and Shape T Cell Responses |
title_fullStr | Lipopolysaccharides with Acylation Defects Potentiate TLR4 Signaling and Shape T Cell Responses |
title_full_unstemmed | Lipopolysaccharides with Acylation Defects Potentiate TLR4 Signaling and Shape T Cell Responses |
title_short | Lipopolysaccharides with Acylation Defects Potentiate TLR4 Signaling and Shape T Cell Responses |
title_sort | lipopolysaccharides with acylation defects potentiate tlr4 signaling and shape t cell responses |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3563657/ https://www.ncbi.nlm.nih.gov/pubmed/23390517 http://dx.doi.org/10.1371/journal.pone.0055117 |
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