Structurally defined helminth glycan-ovalbumin conjugates reveal epitope-dependent dendritic cell uptake.

Authors

Qiang Chao, Yi Jiang, Qianghui Tang, Jianfeng Zhang, Bei Wang, Chunrong Xiong, Bei Zhang, Song Zhao, Kun Yang

Published in

International journal of biological macromolecules. Pages 154557. Sep 19, 2026. Epub Sep 19, 2026.

Abstract

Helminth infections impose a substantial global health burden, with parasite glycoconjugates and their glycan epitopes playing critical roles in host immune recognition and immunomodulation. However, systematic investigation of structure-activity relationships is impeded by the structural complexity and heterogeneity of helminth glycans, limiting the availability of homogeneous materials. Here, we report a modular chemoenzymatic strategy for generating eleven structurally defined helminth glycans bearing signature epitopes, including LacdiNAc (LDN) and fucosylated LacdiNAc (LDNF) terminal motifs, as well as core α1,3-fucose and core β1,2-xylose modifications in N-glycans. A panel of truncated glycosyltransferases (CeGalNAcT, SmFucT-E, ZmXylT, and ZmFucT) expressed in insect cells enabled regio- and stereoselective glycan assembly. Eight representative N-glycans were conjugated to ovalbumin (OVA), labeled with fluorescein isothiocyanate (FITC), and assessed for cellular association and internalization using primary murine bone marrow-derived dendritic cells (BMDCs), with DC2.4 cells employed for comparative characterization. Active internalization was distinguished from surface binding through temperature-controlled uptake assays, confocal microscopy, and receptor inhibition experiments. Terminal epitopes, especially LDNF, significantly promoted dendritic cell uptake compared with OVA-FITC; Under the conditions tested, combining terminal epitopes with core modifications did not further increase uptake relative to terminal epitopes alone. Receptor inhibition experiments supported the involvement of Ca²⁺-dependent glycan recognition and multiple lectin-mediated pathways. Collectively, this work establishes an efficient platform for accessing homogeneous helminth glycans and reveals how defined carbohydrate epitopes shape glycoconjugate recognition by dendritic cells.

PMID:
42762884
Bibliographic data and abstract were imported from PubMed on 20 Sep 2026.

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