<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>105(10)</volume><submitter>Wang SK</submitter><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</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pagination>3690-5</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2268808</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN.</pubmed_title><pmcid>PMC2268808</pmcid><pubmed_authors>Liang PH</pubmed_authors><pubmed_authors>Wong CH</pubmed_authors><pubmed_authors>Wang SK</pubmed_authors><pubmed_authors>Astronomo RD</pubmed_authors><pubmed_authors>Hsieh SL</pubmed_authors><pubmed_authors>Hsu TL</pubmed_authors><pubmed_authors>Burton DR</pubmed_authors></additional><is_claimable>false</is_claimable><name>Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN.</name><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</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Mar</publication><modification>2026-03-16T16:33:55.824Z</modification><creation>2025-08-31T03:05:59.052Z</creation></dates><accession>S-EPMC2268808</accession><cross_references><pubmed>18310320</pubmed><doi>10.1073/pnas.0712326105</doi></cross_references></HashMap>