On-Chip Screening of a Glycomimetic Library with C-Type Lectins Reveals Structural Features Responsible for Preferential Binding of Dectin-2 over DC-SIGN/R and Langerin

Laura Medve; Silvia Achilli; Sonia Serna; Fabio Zuccotto; Norbert Varga; Michel Thépaut; Monica Civera; Corinne Vivès; Franck Fieschi; Niels Reichardt; Anna Bernardi

doi:10.1002/chem.201802577

On-Chip Screening of a Glycomimetic Library with C-Type Lectins Reveals Structural Features Responsible for Preferential Binding of Dectin-2 over DC-SIGN/R and Langerin

Chemistry. 2018 Sep 25;24(54):14448-14460. doi: 10.1002/chem.201802577. Epub 2018 Sep 3.

Authors

Affiliations

¹ Dipartimento di Chimica, Università degli Studi di Milano, Via Golgi 19, 20133, Milano, Italy.
² Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, 38000, Grenoble, France.
³ Glycotechnology laboratory, CIC biomaGUNE, Paseo Miramón 182, 20014, Donostia-San Sebastián, Spain.
⁴ University of Dundee, Dundee, UK.
⁵ CIBER-BBN, 20014, Donostia-San Sebastián, Spain.

Abstract

A library of mannose- and fucose-based glycomimetics was synthesized and screened in a microarray format against a set of C-type lectin receptors (CLRs) that included DC-SIGN, DC-SIGNR, langerin, and dectin-2. Glycomimetic ligands able to interact with dectin-2 were identified for the first time. Comparative analysis of binding profiles allowed their selectivity against other CLRs to be probed.

Keywords: C-type lectins; carbohydrates; drug discovery; glycomimetics; microarrays.

Abstract

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