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

Noelia de la Cruz; Javier Ramos-Soriano; José J. Reina; José L. de Paz; Michel Thépaut; Franck Fieschi; Ana Sousa-Herves; Javier Rojo

doi:10.1039/D0OB01380C

You do not have JavaScript enabled. Please enable JavaScript to access the full features of the site or access our non-JavaScript page.

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

Noelia de la Cruz,^a Javier Ramos-Soriano,*^a José J. Reina,^a José L. de Paz,^a Michel Thépaut,^b Franck Fieschi,^b Ana Sousa-Herves^a and Javier Rojo

*^a

Author affiliations

* Corresponding authors

^a Glycosystems Laboratory, Instituto de Investigaciones Químicas (IIQ), CSIC – Universidad de Sevilla, Av. Américo Vespucio 49, Seville 41092, Spain
E-mail: javiramossoriano@gmail.com, javier.rojo@iiq.csic.es

^b Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000 Grenoble, France

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.

This article is part of the themed collection: Chemical Biology in OBC

Download options Please wait...

Supplementary files

Supplementary information PDF (2053K)

Article information

DOI: https://doi.org/10.1039/D0OB01380C
Article type: Paper
Submitted: 06 Jul 2020
Accepted: 27 Jul 2020
First published: 27 Jul 2020
This article is Open Access

Download Citation

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

Permissions

Request permissions

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

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. You can use material from this article in other publications, without requesting further permission from the RSC, provided that the correct acknowledgement is given and it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party commercial publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Social activity

Fetching data from CrossRef.
This may take some time to load.

Organic & Biomolecular Chemistry