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• W3044007951 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." @default.
• W3044007951 created "2020-07-29" @default.
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• W3044007951 date "2020-01-01" @default.
• W3044007951 modified "2023-10-15" @default.
• W3044007951 title "Influence of the reducing-end anomeric configuration of the Man₉ epitope on DC-SIGN recognition" @default.
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• W3044007951 doi "https://doi.org/10.1039/d0ob01380c" @default.
• W3044007951 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32729597" @default.
• W3044007951 hasPublicationYear "2020" @default.
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