Issue 31, 2020

Influence of the reducing-end anomeric configuration of the Man9 epitope on DC-SIGN recognition

Abstract

High-mannose (Man9GlcNAc2) is the main carbohydrate unit present in viral envelope glycoproteins such as gp120 of HIV and the GP1 of Ebola virus. This oligosaccharide comprises the Man9 epitope conjugated to two terminal N-acetylglucosamines by otherwise rarely-encountered β-mannose glycosidic bond. Formation of this challenging linkage is the bottleneck of the few synthetic approaches described to prepare high mannose. Herein, we report the synthesis of the Man9 epitope with both alpha and beta configurations at the reducing end, and subsequent evaluation of the impact of this configuration on binding to natural receptor of high-mannose, DC-SIGN. Using fluorescence polarization assays, we demonstrate that both anomers bind to DC-SIGN with comparable affinity. These relevant results therefore indicate that the more synthetically-accesible Man9 alpha epitope may be deployed as ligand for DC-SIGN in both in vitro and in vivo biological assays.

Graphical abstract: Influence of the reducing-end anomeric configuration of the Man9 epitope on DC-SIGN recognition

Supplementary files

Article information

Article type
Paper
Submitted
06 Jul 2020
Accepted
27 Jul 2020
First published
27 Jul 2020
This article is Open Access
Creative Commons BY-NC license

Org. Biomol. Chem., 2020,18, 6086-6094

Influence of the reducing-end anomeric configuration of the Man9 epitope on DC-SIGN recognition

N. de la Cruz, J. Ramos-Soriano, J. J. Reina, J. L. de Paz, M. Thépaut, F. Fieschi, A. Sousa-Herves and J. Rojo, Org. Biomol. Chem., 2020, 18, 6086 DOI: 10.1039/D0OB01380C

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