About: Fasciola hepatica glycoconjugates immuneregulate dendritic cells through the Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin inducing T cell anergy

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Fasciola hepatica glycoconjugates immuneregulate dendritic cells through the Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin inducing T cell anergy Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Fasciola hepatica glycoconjugates immuneregulate dendritic cells through the Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin inducing T cell anergy
Creator	Brossard, Natalie Freire, Teresa Giacomini, Cecilia Kalay, Hakan Noya, Verónica Rodríguez, Ernesto García-Vallejo, Juan Van Kooyk, Yvette
Source	Medline; PMC
abstract	Dendritic cell-specific ICAM-3 grabbing non-integrin (DC-SIGN) expressed on a variety of DCs, is a C-type lectin receptor that recognizes glycans on a diverse range of pathogens, including parasites. The interaction of DC-SIGN with pathogens triggers specific signaling events that modulate DC-maturation and activity and regulate T-cell activation by DCs. In this work we evaluate whether F. hepatica glycans can immune modulate DCs via DC-SIGN. We demonstrate that DC-SIGN interacts with F. hepatica glycoconjugates through mannose and fucose residues. We also show that mannose is present in high-mannose structures, hybrid and trimannosyl N-glycans with terminal GlcNAc. Furthermore, we demonstrate that F. hepatica glycans induce DC-SIGN triggering leading to a strong production of TLR-induced IL-10 and IL-27p28. In addition, parasite glycans induced regulatory DCs via DC-SIGN that decrease allogeneic T cell proliferation, via the induction of anergic/regulatory T cells, highlighting the role of DC-SIGN in the regulation of innate and adaptive immune responses by F. hepatica. Our data confirm the immunomodulatory properties of DC-SIGN triggered by pathogen-derived glycans and contribute to the identification of immunomodulatory glyans of helminths that might eventually be useful for the design of vaccines against fasciolosis.
has issue date	2017-04-24(xsd:dateTime)
bibo:doi	10.1038/srep46748
bibo:pmid	28436457
has license	cc-by
sha1sum (hex)	105eabe3e019ae2bb0f93493d7f43d2c1c19e4c5
schema:url	https://doi.org/10.1038/srep46748
resource representing a document's title	Fasciola hepatica glycoconjugates immuneregulate dendritic cells through the Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin inducing T cell anergy
has PubMed Central identifier	PMC5402274
has PubMed identifier	28436457
schema:publication	Sci Rep
resource representing a document's body	covid:105eabe3e019ae2bb0f93493d7f43d2c1c19e4c5#body_text
is schema:about of	named entity 'DC-SIGN' named entity 'induce' named entity 'residues' named entity 'range' named entity 'GlcNAc' named entity 'triggered' named entity 'IL-10' named entity 'triggers' named entity 'interaction' named entity 'regulatory T cells' named entity 'modulate' named entity 'innate' named entity 'C-type lectin receptor' named entity 'production' named entity 'F. hepatica' named entity 'F. hepatica' named entity 'regulatory T cells' named entity 'DCs' named entity 'DC-SIGN' named entity 'TLR' named entity 'GlcNAc' named entity 'glycans' named entity 'F. hepatica' named entity 'fasciolosis' named entity 'Intercellular adhesion molecule' named entity 'DC-SIGN' named entity 'DCs' named entity 'IL-10' named entity 'jack bean' named entity 'DC-SIGN' named entity 'F. hepatica' named entity 'DC-SIGN' named entity 'DC-SIGN' named entity 'liver' named entity 'glycoconjugates' named entity 'assay' named entity 'fully activated' named entity 'DC-SIGN' named entity 'regulating the expression' named entity 'pathogen' named entity 'Real-time PCR' named entity 'parasites' named entity 'Dectin' named entity 'Scientific RepoRts' named entity 'sonicated' named entity 'IL-7' named entity 'cell surface' named entity 'N-glycans' named entity 'host immunity' named entity 'DCs' named entity 'DC-SIGN' named entity 'oligosaccharides' named entity 'DC-SIGN' named entity 'DCs' named entity 'Netherlands' named entity 'Mycobacterium tuberculosis' named entity 'DC-SIGN' named entity 'pathogens' named entity 'DCs' named entity 'TLR' named entity 'N-glycans' named entity 'immune modulation' named entity 'secretion' named entity 'DCs' named entity 'chelating agent' named entity 'antibodies' named entity 'Lonza' named entity 'Amsterdam' named entity 'glycans' named entity 'antibodies' named entity 'monocytes' named entity 'DCs' named entity 'LPS' named entity 'interact'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software