Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin

DC-SIGN, a lectin, which presents at the surface of immature dendritic cells, constitutes nowadays a promising target for the design of new antiviral drugs. This lectin recognizes highly glycosylated proteins present at the surface of several pathogens such as HIV, Ebola virus, Candida albicans, Myc...

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Autores: Reina, José J., Díaz, Irene, Nieto, Pedro M., Campillo, Nuria Eugenia, Páez, Juan Antonio, Tabarani, Georges, Fieschi, Franck, Rojo, Javier
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2008
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/73498
Acceso en línea:https://hdl.handle.net/11441/73498
https://doi.org/10.1039/b802144a
Access Level:acceso abierto
Palabra clave:Cell adhesion molecules
Lectins
C-type
Mannose
Receptors
Cell surface
Trisaccharides
Ligands
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spelling Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectinReina, José J.Díaz, IreneNieto, Pedro M.Campillo, Nuria EugeniaPáez, Juan AntonioTabarani, GeorgesFieschi, FranckRojo, JavierCell adhesion moleculesLectinsC-typeMannoseReceptorsCell surfaceTrisaccharidesLigandsDC-SIGN, a lectin, which presents at the surface of immature dendritic cells, constitutes nowadays a promising target for the design of new antiviral drugs. This lectin recognizes highly glycosylated proteins present at the surface of several pathogens such as HIV, Ebola virus, Candida albicans, Mycobacterium tuberculosis, etc. Understanding the binding mode of this lectin is a topic of tremendous interest and will permit a rational design of new and more selective ligands. Here, we present computational and experimental tools to study the interaction of di- and trisaccharides with DC-SIGN. Docking analysis of complexes involving mannosyl di- and trisaccharides and the carbohydrate recognition domain (CRD) of DC-SIGN have been performed. Trisaccharides Manα1,2[Manα1,6]Man 1 and Manα1,3[Manα1,6]Man 2 were synthesized from an orthogonally protected mannose as a common intermediate. Using these ligands and the soluble extracellular domain (ECD) of DC-SIGN, NMR experiments based on STD and transfer-NOE were performed providing additional information. Conformational analysis of the mannosyl ligands in the free and bound states was done. These studies have demonstrated that terminal mannoses at positions 2 or 3 in the trisaccharides are the most important moiety and present the strongest contact with the binding site of the lectin. Multiple binding modes could be proposed and therefore should be considered in the design of new ligands.Ministerio de Ciencia y Tecnología SAF 2003–08003-CO2Ministerio de Educación y Ciencia SAF 2006–13391-CO3Royal Society of Chemistry (Great Britain)Ministerio de Ciencia y Tecnología (MCYT). EspañaMinisterio de Educación y Ciencia (MEC). España2008info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/73498https://doi.org/10.1039/b802144areponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésOrganic and Biomolecular Chemistry, 6 (15), 2743-2754.http://dx.doi.org/10.1039/b802144ainfo:eu-repo/semantics/openAccessoai:idus.us.es:11441/734982026-06-17T12:51:07Z
dc.title.none.fl_str_mv Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin
title Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin
spellingShingle Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin
Reina, José J.
Cell adhesion molecules
Lectins
C-type
Mannose
Receptors
Cell surface
Trisaccharides
Ligands
title_short Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin
title_full Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin
title_fullStr Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin
title_full_unstemmed Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin
title_sort Docking, synthesis, and NMR studies of mannosyl trisaccharide ligands for DC-SIGN lectin
dc.creator.none.fl_str_mv Reina, José J.
Díaz, Irene
Nieto, Pedro M.
Campillo, Nuria Eugenia
Páez, Juan Antonio
Tabarani, Georges
Fieschi, Franck
Rojo, Javier
author Reina, José J.
author_facet Reina, José J.
Díaz, Irene
Nieto, Pedro M.
Campillo, Nuria Eugenia
Páez, Juan Antonio
Tabarani, Georges
Fieschi, Franck
Rojo, Javier
author_role author
author2 Díaz, Irene
Nieto, Pedro M.
Campillo, Nuria Eugenia
Páez, Juan Antonio
Tabarani, Georges
Fieschi, Franck
Rojo, Javier
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia y Tecnología (MCYT). España
Ministerio de Educación y Ciencia (MEC). España
dc.subject.none.fl_str_mv Cell adhesion molecules
Lectins
C-type
Mannose
Receptors
Cell surface
Trisaccharides
Ligands
topic Cell adhesion molecules
Lectins
C-type
Mannose
Receptors
Cell surface
Trisaccharides
Ligands
description DC-SIGN, a lectin, which presents at the surface of immature dendritic cells, constitutes nowadays a promising target for the design of new antiviral drugs. This lectin recognizes highly glycosylated proteins present at the surface of several pathogens such as HIV, Ebola virus, Candida albicans, Mycobacterium tuberculosis, etc. Understanding the binding mode of this lectin is a topic of tremendous interest and will permit a rational design of new and more selective ligands. Here, we present computational and experimental tools to study the interaction of di- and trisaccharides with DC-SIGN. Docking analysis of complexes involving mannosyl di- and trisaccharides and the carbohydrate recognition domain (CRD) of DC-SIGN have been performed. Trisaccharides Manα1,2[Manα1,6]Man 1 and Manα1,3[Manα1,6]Man 2 were synthesized from an orthogonally protected mannose as a common intermediate. Using these ligands and the soluble extracellular domain (ECD) of DC-SIGN, NMR experiments based on STD and transfer-NOE were performed providing additional information. Conformational analysis of the mannosyl ligands in the free and bound states was done. These studies have demonstrated that terminal mannoses at positions 2 or 3 in the trisaccharides are the most important moiety and present the strongest contact with the binding site of the lectin. Multiple binding modes could be proposed and therefore should be considered in the design of new ligands.
publishDate 2008
dc.date.none.fl_str_mv 2008
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/73498
https://doi.org/10.1039/b802144a
url https://hdl.handle.net/11441/73498
https://doi.org/10.1039/b802144a
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Organic and Biomolecular Chemistry, 6 (15), 2743-2754.
http://dx.doi.org/10.1039/b802144a
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry (Great Britain)
publisher.none.fl_str_mv Royal Society of Chemistry (Great Britain)
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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