The Plasticity of the Carbohydrate Recognition Domain Dictates the Exquisite Mechanism of Binding of Human Macrophage Galactose-Type Lectin.
NMR spectroscopy
immune-related lectins
molecular modeling
molecular recognition
tumor-associated carbohydrate antigens
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
04 Nov 2019
04 Nov 2019
Historique:
received:
17
06
2019
revised:
01
08
2019
pubmed:
14
8
2019
medline:
14
11
2019
entrez:
13
8
2019
Statut:
ppublish
Résumé
The human macrophage galactose-type lectin (MGL), expressed on macrophages and dendritic cells (DCs), modulates distinct immune cell responses by recognizing N-acetylgalactosamine (GalNAc) containing structures present on pathogens, self-glycoproteins, and tumor cells. Herein, NMR spectroscopy and molecular dynamics (MD) simulations were used to investigate the structural preferences of MGL against different GalNAc-containing structures derived from the blood group A antigen, the Forssman antigen, and the GM2 glycolipid. NMR spectroscopic analysis of the MGL carbohydrate recognition domain (MGL-CRD, C181-H316) in the absence and presence of methyl α-GalNAc (α-MeGalNAc), a simple monosaccharide, shows that the MGL-CRD is highly dynamic and its structure is strongly altered upon ligand binding. This plasticity of the MGL-CRD structure explains the ability of MGL to accommodate different GalNAc-containing molecules. However, key differences are observed in the recognition process depending on whether the GalNAc is part of the blood group A antigen, the Forssman antigen, or GM2-derived structures. These results are in accordance with molecular dynamics simulations that suggest the existence of a distinct MGL binding mechanism depending on the context of GalNAc moiety presentation. These results afford new perspectives for the rational design of GalNAc modifications that fine tune MGL immune responses in distinct biological contexts, especially in malignancy.
Identifiants
pubmed: 31404475
doi: 10.1002/chem.201902780
doi:
Substances chimiques
Blood Group Antigens
0
Lectins, C-Type
0
Ligands
0
MGL lectin, human
0
Recombinant Proteins
0
Acetylgalactosamine
KM15WK8O5T
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
13945-13955Subventions
Organisme : Fundação para a Ciência e a Tecnologia
ID : PTDC/BIA-MIB/31028/2017
Organisme : Fundação para a Ciência e a Tecnologia
ID : IF/00780/2015
Organisme : Fundação para a Ciência e a Tecnologia
ID : UID/Multi/04378/2019
Organisme : Fundação para a Ciência e a Tecnologia
ID : PD/BD/142847/2018
Organisme : Fundação para a Ciência e a Tecnologia
ID : ROTEIRO/0031/2013 - PINFRA/22161/2016
Organisme : Ministry of Science, Innovation and Universities
ID : RTI2018-099592-B-C21
Organisme : European Research Council
ID : 788143-RECGLYCANMR
Pays : International
Organisme : Agencia Estatal de Investigación
ID : CTQ2015-64597-C2-1-P
Organisme : Agencia Estatal de Investigación
ID : SEV-2016-0644
Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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