{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["105(10)"],"submitter":["Wang SK"],"pubmed_abstract":["It is widely accepted that the heavily glycosylated glycoprotein gp120 on the surface of HIV-1 shields peptide epitopes from recognition by the immune system and may promote infection in vivo by interaction with dendritic cells and transport to tissue rich in CD4(+) T cells such as lymph nodes. A conserved cluster of oligomannose glycans on gp120 has been identified as the epitope recognized by the broadly HIV-1-neutralizing monoclonal antibody 2G12. Oligomannose glycans are also the ligands for DC-SIGN, a C-type lectin found on the surface of dendritic cells. Multivalency is fundamental for carbohydrate-protein interactions, and mimicking of the high glycan density on the virus surface has become essential for designing carbohydrate-based HIV vaccines and antiviral agents. We report an ef"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["3690-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2268808"],"repository":["biostudies-literature"],"pubmed_title":["Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN."],"pmcid":["PMC2268808"],"pubmed_authors":["Liang PH","Wong CH","Wang SK","Astronomo RD","Hsieh SL","Hsu TL","Burton DR"],"additional_accession":[]},"is_claimable":false,"name":"Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN.","description":"It is widely accepted that the heavily glycosylated glycoprotein gp120 on the surface of HIV-1 shields peptide epitopes from recognition by the immune system and may promote infection in vivo by interaction with dendritic cells and transport to tissue rich in CD4(+) T cells such as lymph nodes. A conserved cluster of oligomannose glycans on gp120 has been identified as the epitope recognized by the broadly HIV-1-neutralizing monoclonal antibody 2G12. Oligomannose glycans are also the ligands for DC-SIGN, a C-type lectin found on the surface of dendritic cells. Multivalency is fundamental for carbohydrate-protein interactions, and mimicking of the high glycan density on the virus surface has become essential for designing carbohydrate-based HIV vaccines and antiviral agents. We report an ef","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Mar","modification":"2026-03-16T16:33:55.824Z","creation":"2025-08-31T03:05:59.052Z"},"accession":"S-EPMC2268808","cross_references":{"pubmed":["18310320"],"doi":["10.1073/pnas.0712326105"]}}