Mascaraque, AinhoaKowalczyk, WioletaFernández, TahiaPalomares, FranciscaMayorga, CristobalinaAndreu, DavidRojo, Javier2024-03-052024-03-052015-102040-2511http://hdl.handle.net/10668/2274http://hdl.handle.net/20.500.12105/18881Mannosylation facilitates uptake and internalization of immunogenic peptides by antigen-processing cells expressing mannose receptors at their surface, such as DC-SIGN, a lectin that plays a key role in the immune response against different pathogens. This internalization, processing and subsequent MHC presentation may result in a strong T cell stimulation. Here, we hypothesized that combining mannose glycodendrons with multivalent presentation of peptide epitopes in a likewise dendron format would yield hybrid constructs, named glycodendropeptides (GDPs), with the capacity to enhance peptide immunogenicity, hence providing a novel and versatile platform for applications in immunotherapy. Thus, GDPs of different valencies displaying the NP366-374 epitope, a conserved sequence from the influenza A virus nucleoprotein (NP), have been built by two click chemistry-based methodologies and assessed as potential flu vaccine candidates. Preliminary evaluation of the ability of these constructs to stimulate dendritic cell maturation and lymphocyte proliferation was promising, showing the highest-functionalized NP366-374 GDPs as inducing the strongest immunostimulatory effect.engVoRhttp://creativecommons.org/licenses/by-nd/4.0/Moléculas de adhesión celularQuímica clicSecuencia conservadaDendrómerosCélulas dendróticasEpítoposInmunoterapiaLectinas tipo CManosaLectinas de unión a manosaPéptidosProteínas de unión al ARNReceptores de superficie celularLinfocitos TVacunasProteínas del centro víricoCell Adhesion MoleculesClick ChemistryConserved SequenceDendrimersDendritic CellsEpitopesImmunotherapyLectins, C-TypeMannoseMannose-Binding LectinsPeptidesRNA-Binding ProteinsReceptors, Cell SurfaceT-LymphocytesVaccinesViral Core ProteinsAttribution-NoDerivs 4.0 International610.1039/C5MD00133A2040-2503MedChemCommopen access