Influence of the reducing-end anomeric configuration of the Man9 epitope on DC-SIGN recognition
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....
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| Veröffentlicht in: | Organic & biomolecular chemistry 2020-08, Vol.18 (31), p.6086-6094 |
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| container_issue | 31 |
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| container_title | Organic & biomolecular chemistry |
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| creator | de la Cruz, Noelia Ramos-Soriano, Javier Reina, José J de Paz, José L Thépaut, Michel Fieschi, Franck Sousa-Herves, Ana Rojo, Javier |
| description | 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. |
| doi_str_mv | 10.1039/d0ob01380c |
| format | Article |
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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. 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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.</description><subject>Carbohydrates</subject><subject>Configurations</subject><subject>DC-SIGN protein</subject><subject>Epitopes</subject><subject>Fluorescence</subject><subject>Fluorescence polarization</subject><subject>Glycoprotein gp120</subject><subject>Glycoproteins</subject><subject>HIV</subject><subject>Human immunodeficiency virus</subject><subject>Mannose</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Oligosaccharides</subject><subject>Viral diseases</subject><subject>Viruses</subject><issn>1477-0520</issn><issn>1477-0539</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNpdzjtPwzAUBWALgUQpLPwCSywsgWs7ju0RFSiVCgx0r5Kb6-IqtUMe_58gHgPTPcN3ji5jlwJuBCh3W0OqQCgLeMRmIjcmA63c8V-WcMrO-n4PIJwp8hnbrqJvRopIPHk-vBPvqB4xxF1GseZlTAfqAnJM0Yfd2JVDSPGXPpfRcWrDkNqpHvn9IntbLV-mCUy7GL7oOTvxZdPTxc-ds83jw2bxlK1fl6vF3TprncFMSmlz8Ki0NBXmutaVdlYDFkoUSubeobEayaAVGtFbSdJWBRCY2lhfqjm7_p5tu_QxUj9sD6FHapoyUhr7rcylA11oKyd69Y_u09jF6blJKWksgAP1CfFOYhs</recordid><startdate>20200821</startdate><enddate>20200821</enddate><creator>de la Cruz, Noelia</creator><creator>Ramos-Soriano, Javier</creator><creator>Reina, José J</creator><creator>de Paz, José L</creator><creator>Thépaut, Michel</creator><creator>Fieschi, Franck</creator><creator>Sousa-Herves, Ana</creator><creator>Rojo, Javier</creator><general>Royal Society of Chemistry</general><scope>7QO</scope><scope>7T7</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20200821</creationdate><title>Influence of the reducing-end anomeric configuration of the Man9 epitope on DC-SIGN recognition</title><author>de la Cruz, Noelia ; Ramos-Soriano, Javier ; Reina, José J ; de Paz, José L ; Thépaut, Michel ; Fieschi, Franck ; Sousa-Herves, Ana ; Rojo, Javier</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p97c-222840fc3527bc45d5b59850c6316324f9c785ce7c815ccf82e28b60e07d78fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Carbohydrates</topic><topic>Configurations</topic><topic>DC-SIGN protein</topic><topic>Epitopes</topic><topic>Fluorescence</topic><topic>Fluorescence polarization</topic><topic>Glycoprotein gp120</topic><topic>Glycoproteins</topic><topic>HIV</topic><topic>Human immunodeficiency virus</topic><topic>Mannose</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Oligosaccharides</topic><topic>Viral diseases</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>de la Cruz, Noelia</creatorcontrib><creatorcontrib>Ramos-Soriano, Javier</creatorcontrib><creatorcontrib>Reina, José J</creatorcontrib><creatorcontrib>de Paz, José L</creatorcontrib><creatorcontrib>Thépaut, Michel</creatorcontrib><creatorcontrib>Fieschi, Franck</creatorcontrib><creatorcontrib>Sousa-Herves, Ana</creatorcontrib><creatorcontrib>Rojo, Javier</creatorcontrib><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Organic & biomolecular chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>de la Cruz, Noelia</au><au>Ramos-Soriano, Javier</au><au>Reina, José J</au><au>de Paz, José L</au><au>Thépaut, Michel</au><au>Fieschi, Franck</au><au>Sousa-Herves, Ana</au><au>Rojo, Javier</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Influence of the reducing-end anomeric configuration of the Man9 epitope on DC-SIGN recognition</atitle><jtitle>Organic & biomolecular chemistry</jtitle><date>2020-08-21</date><risdate>2020</risdate><volume>18</volume><issue>31</issue><spage>6086</spage><epage>6094</epage><pages>6086-6094</pages><issn>1477-0520</issn><eissn>1477-0539</eissn><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.</abstract><cop>Cambridge</cop><pub>Royal Society of Chemistry</pub><doi>10.1039/d0ob01380c</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Organic & biomolecular chemistry, 2020-08, Vol.18 (31), p.6086-6094 |
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| source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Carbohydrates Configurations DC-SIGN protein Epitopes Fluorescence Fluorescence polarization Glycoprotein gp120 Glycoproteins HIV Human immunodeficiency virus Mannose NMR Nuclear magnetic resonance Oligosaccharides Viral diseases Viruses |
| title | Influence of the reducing-end anomeric configuration of the Man9 epitope on DC-SIGN recognition |
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