English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Open

Presents the pdf analysis as premium feature

PDF Analysis

Insights

Presents the summarisation as premium feature

Summarisation

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

The parasitic worm,  Schistosoma mansoni , expresses unusual fucosylated glycans in a stage‐dependent manner that can be recognized by the human innate immune receptor DC‐SIGN, thereby shaping host immune responses. We have developed a synthetic approach for mono‐ and bis‐fucosylated LacdiNAc (LDN‐F and LDN‐DF, respectively), which are epitopes expressed on glycolipids and glycoproteins of  S. mansoni . It is based on the use of monosaccharide building blocks having carefully selected amino‐protecting groups, facilitating high yielding and stereoselective glycosylations. The molecular interaction between the synthetic glycans and DC‐SIGN was studied by NMR and molecular modeling, which demonstrated that the α1,3‐fucoside of LDN‐F can coordinate with the Ca 2+ ‐ion of the canonical binding site of DC‐SIGN allowing for additional interactions with the underlying LDN backbone. The 1,2‐fucoside of LDN‐DF can be complexed in a similar manner, however, in this binding mode GlcNAc and GalNAc of the LDN backbone are placed away from the protein surface resulting in a substantially lower binding affinity. Glycan microarray binding studies showed that the avidity and selectivity of binding is greatly enhanced when the glycans are presented multivalently, and in this format Le x  and LDN‐F gave strong responsiveness, whereas no binding was detected for LDN‐DF. The data indicates that  S. mansoni  has developed a strategy to avoid detection by DC‐SIGN in a stage‐dependent manner by the addition of a fucoside to a number of its ligands.

Mono‐ and Di‐Fucosylated Glycans of the Parasitic Worm S. mansoni are Recognized Differently by the Innate Immune Receptor DC‐SIGN