Chemo‐Enzymatic Synthesis of S. mansoni O‐Glycans and Their Evaluation as Ligands for C‐Type Lectin Receptors MGL, DC‐SIGN, and DC‐SIGNR. Issue 56 (17th September 2020)

• Record Type: Journal Article
• Authors: Pham, Julie; Hernandez, Alvaro; Cioce, Anna; Achilli, Silvia; Goti, Giulio; Vivès, Corinne; Thepaut, Michel; Bernardi, Anna; Fieschi, Franck; Reichardt, Niels‐Christian
• Is Part Of: Chemistry. Volume 26:Issue 56(2020)
• Page Start: 12818
• Page End: 12830
• Publication Date: 2020-09-17
• Subjects: carbohydrates -- enzymes -- glycoconjugates -- lectins -- microarrays; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.202000291
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: Due to their interactions with C‐type lectin receptors (CLRs), glycans from the helminth Schistosoma mansoni represent promising leads for treatment of autoimmune diseases, allergies or cancer. We chemo‐enzymatically synthesized nine O‐glycans based on the two predominant O‐glycan cores observed in the infectious stages of schistosomiasis, the mucin core 2 and the S. mansoni core. The O‐glycans were fucosylated next to a selection of N ‐glycans directly on a microarray slide using a recombinant fucosyltransferase and GDP‐fucose or GDP‐6‐azidofucose as donor. Binding assays with fluorescently labelled human CLRs DC‐SIGN, DC‐SIGNR and MGL revealed the novel O‐glycan O8 as the best ligand for MGL from our panel. Significant binding to DC‐SIGN was also found for azido‐fucosylated glycans. Contrasting binding specificities were observed between the monovalent carbohydrate recognition domain (CRD) and the tetravalent extracellular domain (ECD) of DC‐SIGNR. Abstract : A series of parasite O‐glycans structures have been prepared by chemoenzymatic synthesis and their affinity towards several C‐type lectins screened using glycan arrays.