Synthesis and Microarray-Assisted Binding Studies of Core Xylose and Fucose Containing N‑Glycans Katarzyna Brzezicka Begoña Echeverria Sonia Serna Angela van Diepen Cornelis H. Hokke Niels-Christian Reichardt 10.1021/cb501023u.s001 https://acs.figshare.com/articles/journal_contribution/Synthesis_and_Microarray_Assisted_Binding_Studies_of_Core_Xylose_and_Fucose_Containing_N_Glycans/2166256 The synthesis of a collection of 33 xylosylated and core-fucosylated N-glycans found only in nonmammalian organisms such as plants and parasitic helminths has been achieved by employing a highly convergent chemo-enzymatic approach. The influence of these core modifications on the interaction with plant lectins, with the human lectin DC-SIGN (Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Nonintegrin), and with serum antibodies from schistosome-infected individuals was studied. Core xylosylation markedly reduced or completely abolished binding to several mannose-binding plant lectins and to DC-SIGN, a C-type lectin receptor present on antigen presenting cells. Employing the synthetic collection of core-fucosylated and core-xylosylated N-glycans in the context of a larger glycan array including structures lacking these core modifications, we were able to dissect core xylose and core fucose specific antiglycan antibody responses in <i>S. mansoni</i> infection sera, and we observed clear and immunologically relevant differences between children and adult groups infected with this parasite. The work presented here suggests that, quite similar to bisecting N-acetylglucosamine, core xylose distorts the conformation of the unsubstituted glycan, with important implications for the immunogenicity and protein binding properties of complex N-glycans. 2015-05-15 00:00:00 core modifications lectin mansoni infection sera antiglycan antibody responses dissect core xylose protein binding properties