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

Angewandte Chemie, vol. 135

Abstract

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.

Authors 8

1. Sandra Behren

   Umeå University · Leibniz Institute for Analytical Sciences - ISAS

   Affiliation as printed

   Department of Chemistry Umeå University 90187 Umeå Sweden

   Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V. 44227 Dortmund Germany

2. Jin Yu

   Imperial College London · Leibniz Institute for Analytical Sciences - ISAS

   Affiliation as printed

   Glycosciences Laboratory Imperial College London London W12 0NN UK

   Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V. 44227 Dortmund Germany

   Imperial College London Faculty of Medicine, Glycoscience laboratory, UNITED KINGDOM

3. Christian Pett

   Umeå University · Leibniz Institute for Analytical Sciences - ISAS

   Affiliation as printed

   Department of Chemistry Umeå University 90187 Umeå Sweden

   Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V. 44227 Dortmund Germany

4. Manuel Schorlemer

   Umeå University · Leibniz Institute for Analytical Sciences - ISAS

   Affiliation as printed

   Department of Chemistry Umeå University 90187 Umeå Sweden

   Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V. 44227 Dortmund Germany

5. Viktoria Heine Aachen

   RWTH Aachen University

   Affiliation as printed

   Laboratory for Biomaterials Institute of Biotechnology and Helmholtz-Institute for Biomedical Engineering RWTH Aachen University Pauwelsstraße 20 52074 Aachen Germany

6. Thomas Fischöder Aachen

   RWTH Aachen University

   Affiliation as printed

   Laboratory for Biomaterials Institute of Biotechnology and Helmholtz-Institute for Biomedical Engineering RWTH Aachen University Pauwelsstraße 20 52074 Aachen Germany

7. Lothar Elling Aachen

   RWTH Aachen University

   Affiliation as printed

   Laboratory for Biomaterials Institute of Biotechnology and Helmholtz-Institute for Biomedical Engineering RWTH Aachen University Pauwelsstraße 20 52074 Aachen Germany

8. Ulrika Westerlind corresponding

   Umeå University · Leibniz Institute for Analytical Sciences - ISAS

   Affiliation as printed

   Department of Chemistry Umeå University 90187 Umeå Sweden

   Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V. 44227 Dortmund Germany