Envelope surface glycoprotein gp120
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env
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HIV-1 SF162 or LAI Env (gp140) binds to CD209 (DC-SIGN) |
PubMed
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env
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HIV-1 Env (gp120) binds to CD209 (DC-SIGN), which induces NFKB1 (NF-kB), MAPK1 (ERK1/2), and MAPK14 (p38) |
PubMed
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env
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HIV-1 JRFL and HXB2 (gp120) binds CD209 (DC-SIGN) |
PubMed
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env
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A dendritic cells (DC)-specific C-type lectin, DC-SIGN, is highly expressed on DC present in mucosal tissues, binds to the HIV-1 envelope glycoprotein gp120, and facilitates infection of HIV-1 permissive cells in trans |
PubMed
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env
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HIV-1 Env gp120/41 (JRFL Env in the contaxt of HIV-Gag-GFP VLP) binds to CD209 (DC-SIGN) on the surface of basophils |
PubMed
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env
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The N-terminal DC-SIGN CRD region (residues 253-288) is essential for HIV-1 binding and transmission and Y258 is required for these activities, suggesting the N-terminal CRD region involves the interaction of DC-SIGN with gp120 |
PubMed
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Natural antibodies against the carbohydrate recognition domain (CRD) of DC-SIGN block the attachment of HIV-1 to DC-SIGN-positive cells and inhibit transmission in trans of HIV-1 to T cells, suggesting the CRD is important for its interaction with gp120 |
PubMed
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Binding of HIV-1 gp120 to DC-SIGN leads to excessive ASK-1 activation and promotes ASK-1-dependent apoptosis in human dendritic cells |
PubMed
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env
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Binding of HIV-1 gp120 to DC-SIGN sensitizes monocyte-derived dendritic cells for CD40L-mediated apoptosis |
PubMed
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env
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HIV-1 gp120 downregulates HIV-1 Nef dependent IL-6 release, which requires the interaction of gp120 with DC-SIGN in immature dentritic cells |
PubMed
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env
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CD4-linker-DC-SIGN fusion proteins enhance binding affinity to HIV-1 gp140 and gp120 in comparison to sCD4 and sDC-SIGN. These fusion proteins inhibit HIV-1 capture and transfer via DC-SIGN-expressing cells and iMDDCs |
PubMed
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env
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DC-SIGN is strongly upregulated in M2a-polarized monocyte-derived-macrophages (MDMs), which leads to facilitate HIV-1 entry via gp120/gp41 and DNA synthesis in M2a-MDMs and to efficiently transmit both R5 and X4 HIV-1 to CD4+ T cells |
PubMed
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env
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Enrichment of oligomannose N-glycans on HIV-1 gp120 enhances DC-SIGN binding but reduces the subsequent transmission to target cells |
PubMed
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env
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DC-SIGN engagement by HIV-1 gp120 on dendritic cell (DC) surface subsequently activates Cdc42, Pak1, and Wasp, leading to an increase in membrane extensions at the DC surface |
PubMed
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env
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AM3 (Inmunoferon) inhibits the interaction of DC-SIGN with both ICAM3 and HIV-1 gp120 protein and blocks the DC-SIGN-dependent capture of HIV virions and the HIV trans-infection capability of DC-SIGN transfectants |
PubMed
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env
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Raji-DC-SIGN cells preferentially enhance CXCR4 usage of dual-tropic HIV-1 with higher V3 charges in gp120 |
PubMed
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env
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DC-SIGN triacidic cluster (353EEE355) mutant is impaired in receptor-mediated endocytosis of HIV-1 gp120 in transfected human myeloid K-562 cells |
PubMed
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env
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One HIV-1 gp120 triple glycosylation mutant form 134mut (carrying N293Q, N382Q, and N388Q mutations in gp120) exhibits a significant increase in sensitivity to both mannan competition and endoglycosidase H digestion in a DC-SIGN binding assay |
PubMed
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env
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Mermaid shares glycan specificity with DC-SIGN and inhibits the interaction between DC-SIGN and HIV-1 gp120 |
PubMed
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env
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Oligomannose glycans play as ligands for DC-SIGN, and can inhibit the binding of gp120 to 2G12 and recombinant dimeric DC-SIGN |
PubMed
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env
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End-stage CCR5-tropic HIV-1 have a reduced ability to use DC-SIGN resulting from the loss of potential N-linked glycosylation sites (PNGS) in the gp120 V2 and V4 regions, which are present in the majority of chronic stage CCR5-tropic variants |
PubMed
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env
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Expression of CD4 on Raji B cells strongly inhibits DC-SIGN-mediated HIV-1 (gp120) transmission to T cells; co-expression of CD4 and DC-SIGN in Raji cells promotes internalization and intracellular retention of HIV-1 |
PubMed
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env
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Monoclonal antibodies produced from hybridoma clones recognize DC-SIGN on monocyte-derived dendritic cells and on dermal-type macrophages to interfere with DC-SIGN binding to HIV-1 gp120 |
PubMed
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env
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Glycopolymers effectively prevent the interactions between a human dendritic cell associated lectin (DC-SIGN) and the HIV-1 gp120 |
PubMed
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env
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HIV-1 gp120 N275Q or N351Q mutants isolated from recombinant CRF07_BC decrease significantly to the DC-SIGN-binding capacity, indicating that the N275 and N351 glycan sites mediate the interaction between CRF07_BC gp120 and DC-SIGN |
PubMed
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env
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Using an siRNA approach indicates DC-SIGN is not required for efficient trans-enhancement of HIV-1 (gp120) infectivity by dendritic cells (DCs) |
PubMed
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env
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Bile salt-stimulated lipase (BSSL) isolated from human milk binds to DC-SIGN, preventing HIV-1 gp120 from interacting with this receptor |
PubMed
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env
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HIV-1 gp120 binds to B cells through mannose C-type lectin receptors (MCLRs), such as DC-SIGN, mannose receptor, and langerin |
PubMed
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env
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Interaction of gp120 with DC-SIGN activates Raf-1 and phosphorylates Raf-1 at positions Ser338, Tyr340, and Tyr341 |
PubMed
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env
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DC-SIGN-mediated blockage of HIV budding is due to internalization of gp120 by DC-SIGN. The 364 amino-acid residues of extracellular and transmembrane domains in DC-SIGN are essential for the blockage |
PubMed
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env
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Human milk oligosaccharides reduce HIV-1-gp120 binding to dendritic cell-specific ICAM3-grabbing non-integrin (DC-SIGN) |
PubMed
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env
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Crystal structures of carbohydrate-recognition domains of DC-SIGN and of DC-SIGNR in combination with binding studies reveal that these receptors selectively recognize endogenous high-mannose oligosaccharides of HIV-1 gp120 |
PubMed
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env
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The cis expression of DC-SIGN on multiple lymphoid cell lines enables more efficient entry and replication of CXCR4-tropic and CCR5/CXCR4 dual-tropic HIV-1 through its binding to the HIV-1 gp120-CD4-CXCR4 complex |
PubMed
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env
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Bovine lactoferrin (bLF) binds strongly to DC-SIGN, thus blocking the interaction between DC-SIGN and HIV-1 gp120 and preventing virus capture and subsequent transmission; bLF is a much more efficient inhibitor of transmission than human lactoferrin |
PubMed
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Binding of HIV-1 gp120 to DC-SIGN does not result in increased adhesion levels of LFA-1 to its ligand ICAM-1 in both immature dendritic cells (DC) and Raji-DC-SIGN cells |
PubMed
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DC-SIGN tetramers are essential for high affinity interactions with the HIV-1 high mannose glycoprotein gp120 |
PubMed
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Mutagenesis of conserved residues (Gly-346, Glu-347, Asn-349, Glu-354, and Asp-355) of DC-SIGN significantly compromises binding to HIV-1 gp120 |
PubMed
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DC-SIGN and MBL bind primarily to glycans on HIV-1 gp120/gp41; preincubation of CXCR4-, CCR5- or dual-tropic HIV-1 strains with MBL prevents DC-SIGN-mediated trans infection of T cells |
PubMed
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env
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The HIV-1 gp120 binding site in DC-SIGN is different from that of ICAM-2 and ICAM-3; alanine-scanning mutagenesis of DC-SIGN at N311, R345, V351, G352, E353, S360, G361, and N362 abrogate ICAM-2/3 binding, whereas the HIV-1 gp120 interaction is unaffected |
PubMed
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Envelope surface glycoprotein gp160, precursor
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env
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Colorectal mucus binds DC-SIGN, which prevents HIV-1 gp140 from binding to DC-SIGN |
PubMed
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env
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CD4-linker-DC-SIGN fusion proteins enhance binding affinity to HIV-1 gp140 and gp120 in comparison to sCD4 and sDC-SIGN. These fusion proteins inhibit HIV-1 capture and transfer via DC-SIGN-expressing cells and iMDDCs |
PubMed
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env
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Enrichment of oligomannose N-glycans on HIV-1 gp140 enhances DC-SIGN binding but reduces the subsequent transmission to target cells |
PubMed
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env
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DC-SIGN binding to the HIV envelope protein effectively increases exposure of the CD4 binding site, which leads to enhance the relative rate of infection of the CD4-dependent strain |
PubMed
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env
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DC-SIGN increases the binding affinity of trimeric gp140 envelope glycoproteins to CD4 on permissive cell surface |
PubMed
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Nef
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nef
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HIV-1 gp120 downregulates HIV-1 Nef dependent IL-6 release, which requires the interaction of gp120 with DC-SIGN in immature dentritic cells |
PubMed
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nef
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Mutation of the dileucine motif at amino acids 165-166 of HIV-1 Nef abolishes the Nef-mediated upregulation of DC-SIGN on the surface of HIV-1 infected dendritic cells |
PubMed
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nef
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HIV-1 Nef upregulates DC-SIGN in HIV-1 infected dendritic cells by inhibiting DC-SIGN endocytosis, which dramatically increases clustering of dendritic cells with T lymphocytes, thereby enhancing HIV-1 transmission |
PubMed
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nef
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Substitution of HIV-1 Nef acidic residue E160 with uncharged residues impairs the ability of Nef to upregulate the expression of DC-SIGN and the invariant chain of MHC class II at the cell surface |
PubMed
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