Molecular basis for intestinal mucin ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Molecular basis for intestinal mucin recognition by galectin-3 and C-type lectins
Auteur(s) :
Leclaire, Charlotte [Auteur]
Lecointe, Karine [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Gunning Patrick, A [Auteur]
Tribolo, Sandra [Auteur]
Kavanaugh Devon, W [Auteur]
Wittmann, Alexandra [Auteur]
Latousakis, Dimitrios [Auteur]
Mackenzie Donald, A [Auteur]
Kawasaki, Norihito [Auteur]
Juge, Nathalie [Auteur]
Lecointe, Karine [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Gunning Patrick, A [Auteur]
Tribolo, Sandra [Auteur]
Kavanaugh Devon, W [Auteur]
Wittmann, Alexandra [Auteur]
Latousakis, Dimitrios [Auteur]
Mackenzie Donald, A [Auteur]
Kawasaki, Norihito [Auteur]
Juge, Nathalie [Auteur]
Titre de la revue :
FASEB Journal
Nom court de la revue :
Faseb J.
Numéro :
32
Pagination :
3301-3320
Date de publication :
2018-06
ISSN :
0892-6638
Mot(s)-clé(s) :
mucus
immune system
N-glycosylation
O-glycosylation
immune system
N-glycosylation
O-glycosylation
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
Intestinal mucins trigger immune responses upon recognition by dendritic cells via protein–carbohydrate interactions. We used a combination of structural, biochemical, biophysical, and cell-based approaches to decipher the ...
Lire la suite >Intestinal mucins trigger immune responses upon recognition by dendritic cells via protein–carbohydrate interactions. We used a combination of structural, biochemical, biophysical, and cell-based approaches to decipher the specificity of the interaction between mucin glycans and mammalian lectins expressed in the gut, including galectin (Gal)-3 and C-type lectin receptors. Gal-3 differentially recognized intestinal mucins with different O-glycosylation profiles, as determined by mass spectrometry (MS). Modification of mucin glycosylation, via chemical treatment leading to a loss of terminal glycans, promoted the interaction of Gal-3 to poly-N-acetyllactosamine. Specific interactions were observed between mucins and mouse dendritic cell-associated lectin (mDectin)-2 or specific intercellular adhesion molecule–grabbing nonintegrin-related-1 (SIGN-R1), but not mDectin-1, using a cell-reporter assay, as also confirmed by atomic force spectroscopy. We characterized the N-glycosylation profile of mouse colonic mucin (Muc)-2 by MS and showed that the interaction with mDectin-2 was mediated by high-mannose N-glycans. Furthermore, we observed Gal-3 binding to the 3 C-type lectins by force spectroscopy. We showed that mDectin-1, mDectin-2, and SIGN-R1 are decorated by N-glycan structures that can be recognized by the carbohydrate recognition domain of Gal-3. These findings provide a structural basis for the role of mucins in mediating immune responses and new insights into the structure and function of major mammalian lectins.—Leclaire, C., Lecointe, K., Gunning, P. A., Tribolo, S., Kavanaugh, D. W., Wittmann, A., Latousakis, D., MacKenzie, D. A., Kawasaki, N., Juge, N. Molecular basis for intestinal mucin recognition by galectin-3 and C-type lectins. FASEB J. 32, 3301–3320 (2018). www.fasebj.orgLire moins >
Lire la suite >Intestinal mucins trigger immune responses upon recognition by dendritic cells via protein–carbohydrate interactions. We used a combination of structural, biochemical, biophysical, and cell-based approaches to decipher the specificity of the interaction between mucin glycans and mammalian lectins expressed in the gut, including galectin (Gal)-3 and C-type lectin receptors. Gal-3 differentially recognized intestinal mucins with different O-glycosylation profiles, as determined by mass spectrometry (MS). Modification of mucin glycosylation, via chemical treatment leading to a loss of terminal glycans, promoted the interaction of Gal-3 to poly-N-acetyllactosamine. Specific interactions were observed between mucins and mouse dendritic cell-associated lectin (mDectin)-2 or specific intercellular adhesion molecule–grabbing nonintegrin-related-1 (SIGN-R1), but not mDectin-1, using a cell-reporter assay, as also confirmed by atomic force spectroscopy. We characterized the N-glycosylation profile of mouse colonic mucin (Muc)-2 by MS and showed that the interaction with mDectin-2 was mediated by high-mannose N-glycans. Furthermore, we observed Gal-3 binding to the 3 C-type lectins by force spectroscopy. We showed that mDectin-1, mDectin-2, and SIGN-R1 are decorated by N-glycan structures that can be recognized by the carbohydrate recognition domain of Gal-3. These findings provide a structural basis for the role of mucins in mediating immune responses and new insights into the structure and function of major mammalian lectins.—Leclaire, C., Lecointe, K., Gunning, P. A., Tribolo, S., Kavanaugh, D. W., Wittmann, A., Latousakis, D., MacKenzie, D. A., Kawasaki, N., Juge, N. Molecular basis for intestinal mucin recognition by galectin-3 and C-type lectins. FASEB J. 32, 3301–3320 (2018). www.fasebj.orgLire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Inserm
Université de Lille
CHU Lille
Université de Lille
CHU Lille
Équipe(s) de recherche :
Fungal associated invasive and inflammatory diseases
Date de dépôt :
2019-03-01T14:35:11Z
2021-06-14T07:20:28Z
2024-04-17T11:30:59Z
2021-06-14T07:20:28Z
2024-04-17T11:30:59Z