Fluorinated Man9 as a high mannose mimetic to unravel its recogni-tion by DC-SIGN using NMR

Lectins are capable of reading out the structural information contained in carbohydrates through specific recognition processes. Determining the binding epitope of the sugar is fundamental to understanding this recognition event. NMR is a powerful tool to obtain this structural information in soluti...

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Detalles Bibliográficos
Autores: Silva-Díaz, Adrián, Ramírez-Cárdenas, Jonathan, Muñoz-García, Juan C., Fuente, M. Carmen de la, Thépaut, Michel, Fieschi, Franck, Ramos-Soriano, Javier, Angulo, Jesús, Rojo, Francisco Javier
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/343284
Acceso en línea:http://hdl.handle.net/10261/343284
Access Level:acceso abierto
Palabra clave:Carbohydrate-lectin interaction
DC-SIGN
Fluor-mannose
High mannose
NMR
Descripción
Sumario:Lectins are capable of reading out the structural information contained in carbohydrates through specific recognition processes. Determining the binding epitope of the sugar is fundamental to understanding this recognition event. NMR is a powerful tool to obtain this structural information in solution; however, when the sugar involved is a complex oligosaccharide such as high-mannose, the signal overlap found in the NMR spectra precludes an accurate analysis of the interaction. The introduction of tags into these complex oligosaccharides could overcome these problems and facilitate the NMR studies. Here, we show the preparation of the Man9 of high-mannose with some fluorine tags and the study of the interaction with its receptor, DC-SIGN. This fluorinated ligand has allowed us to apply heteronuclear 2D 1H,19F STD-TOCSYreF NMR experiments, using the initial slope approach, which has facilitated the analysis of the Man9/DC-SIGN interaction unequivocally providing the binding epitope.