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