Fucose Binding Motifs on Mucin Core Glycopeptides Impact Bacterial Lectin Recognition **

Abstract: Mucin glycoproteins are essential components of the mucosal barrier, which protects the host from pathogens. Throughout evolution, bacteria have developed strategies to modulate and penetrate this barrier, and cause virulence by interacting with mucin O‐glycans at the epithelial cell‐surface. O‐fucosylated glycan epitopes on mucins are key ligands of many bacterial lectins. Here, a chemoenzymatic synthesis strategy is described to prepare a library of fucosylated mucin core glycopeptides to enable studies of mucin‐interacting and fucose‐binding bacterial lectins. Glycan cores with biologically important Lewis and H‐antigens were prepared decorating the peptide backbone at different sites and densities. The fucosylated mucin glycopeptides were applied in microarray binding studies to explore the importance of glycan core and peptide backbone presentation of these antigens in binding interactions with the P. aeruginosa lectin LecB and the C. difficile toxin A.

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Fucose Binding Motifs on Mucin Core Glycopeptides Impact Bacterial Lectin Recognition ** ; day:17 ; month:05 ; year:2023 ; extent:13
Angewandte Chemie ; (17.05.2023) (gesamt 13)

Creator
Behren, Sandra
Yu, Jin
Pett, Christian
Schorlemer, Manuel
Heine, Viktoria
Fischöder, Thomas
Elling, Lothar
Westerlind, Ulrika

DOI
10.1002/ange.202302437
URN
urn:nbn:de:101:1-2023051715375876479374
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
14.08.2025, 10:47 AM CEST

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