Dectin-1 is essential for reverse transcytosis of glycosylated SIgA-antigen complexes by intestinal M cells.

Intestinal microfold (M) cells possess a high transcytosis capacity and are able to transport a broad range of materials including particulate antigens, soluble macromolecules, and pathogens from the intestinal lumen to inductive sites of the mucosal immune system. M cells are also the primary pathw...

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Autores principales: Nicolas Rochereau, Daniel Drocourt, Eric Perouzel, Vincent Pavot, Pierre Redelinghuys, Gordon D Brown, Gerard Tiraby, Xavier Roblin, Bernard Verrier, Christian Genin, Blaise Corthésy, Stéphane Paul
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Publicado: Public Library of Science (PLoS) 2013
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Acceso en línea:https://doaj.org/article/88f2443e33b84649b846b4d2a4e28821
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spelling oai:doaj.org-article:88f2443e33b84649b846b4d2a4e288212021-11-18T05:37:50ZDectin-1 is essential for reverse transcytosis of glycosylated SIgA-antigen complexes by intestinal M cells.1544-91731545-788510.1371/journal.pbio.1001658https://doaj.org/article/88f2443e33b84649b846b4d2a4e288212013-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24068891/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Intestinal microfold (M) cells possess a high transcytosis capacity and are able to transport a broad range of materials including particulate antigens, soluble macromolecules, and pathogens from the intestinal lumen to inductive sites of the mucosal immune system. M cells are also the primary pathway for delivery of secretory IgA (SIgA) to the gut-associated lymphoid tissue. However, although the consequences of SIgA uptake by M cells are now well known and described, the mechanisms whereby SIgA is selectively bound and taken up remain poorly understood. Here we first demonstrate that both the Cα1 region and glycosylation, more particularly sialic acid residues, are involved in M cell-mediated reverse transcytosis. Second, we found that SIgA is taken up by M cells via the Dectin-1 receptor, with the possible involvement of Siglec-5 acting as a co-receptor. Third, we establish that transcytosed SIgA is taken up by mucosal CX3CR1⁺ dendritic cells (DCs) via the DC-SIGN receptor. Fourth, we show that mucosal and systemic antibody responses against the HIV p24-SIgA complexes administered orally is strictly dependent on the expression of Dectin-1. Having deciphered the mechanisms leading to specific targeting of SIgA-based Ag complexes paves the way to the use of such a vehicle for mucosal vaccination against various infectious diseases.Nicolas RochereauDaniel DrocourtEric PerouzelVincent PavotPierre RedelinghuysGordon D BrownGerard TirabyXavier RoblinBernard VerrierChristian GeninBlaise CorthésyStéphane PaulPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 11, Iss 9, p e1001658 (2013)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Nicolas Rochereau
Daniel Drocourt
Eric Perouzel
Vincent Pavot
Pierre Redelinghuys
Gordon D Brown
Gerard Tiraby
Xavier Roblin
Bernard Verrier
Christian Genin
Blaise Corthésy
Stéphane Paul
Dectin-1 is essential for reverse transcytosis of glycosylated SIgA-antigen complexes by intestinal M cells.
description Intestinal microfold (M) cells possess a high transcytosis capacity and are able to transport a broad range of materials including particulate antigens, soluble macromolecules, and pathogens from the intestinal lumen to inductive sites of the mucosal immune system. M cells are also the primary pathway for delivery of secretory IgA (SIgA) to the gut-associated lymphoid tissue. However, although the consequences of SIgA uptake by M cells are now well known and described, the mechanisms whereby SIgA is selectively bound and taken up remain poorly understood. Here we first demonstrate that both the Cα1 region and glycosylation, more particularly sialic acid residues, are involved in M cell-mediated reverse transcytosis. Second, we found that SIgA is taken up by M cells via the Dectin-1 receptor, with the possible involvement of Siglec-5 acting as a co-receptor. Third, we establish that transcytosed SIgA is taken up by mucosal CX3CR1⁺ dendritic cells (DCs) via the DC-SIGN receptor. Fourth, we show that mucosal and systemic antibody responses against the HIV p24-SIgA complexes administered orally is strictly dependent on the expression of Dectin-1. Having deciphered the mechanisms leading to specific targeting of SIgA-based Ag complexes paves the way to the use of such a vehicle for mucosal vaccination against various infectious diseases.
format article
author Nicolas Rochereau
Daniel Drocourt
Eric Perouzel
Vincent Pavot
Pierre Redelinghuys
Gordon D Brown
Gerard Tiraby
Xavier Roblin
Bernard Verrier
Christian Genin
Blaise Corthésy
Stéphane Paul
author_facet Nicolas Rochereau
Daniel Drocourt
Eric Perouzel
Vincent Pavot
Pierre Redelinghuys
Gordon D Brown
Gerard Tiraby
Xavier Roblin
Bernard Verrier
Christian Genin
Blaise Corthésy
Stéphane Paul
author_sort Nicolas Rochereau
title Dectin-1 is essential for reverse transcytosis of glycosylated SIgA-antigen complexes by intestinal M cells.
title_short Dectin-1 is essential for reverse transcytosis of glycosylated SIgA-antigen complexes by intestinal M cells.
title_full Dectin-1 is essential for reverse transcytosis of glycosylated SIgA-antigen complexes by intestinal M cells.
title_fullStr Dectin-1 is essential for reverse transcytosis of glycosylated SIgA-antigen complexes by intestinal M cells.
title_full_unstemmed Dectin-1 is essential for reverse transcytosis of glycosylated SIgA-antigen complexes by intestinal M cells.
title_sort dectin-1 is essential for reverse transcytosis of glycosylated siga-antigen complexes by intestinal m cells.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/88f2443e33b84649b846b4d2a4e28821
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