Structural Basis for Selective Recognition of Oligosaccharides by DC-SIGN and DC-SIGNR

@article{Feinberg2001StructuralBF,
  title={Structural Basis for Selective Recognition of Oligosaccharides by DC-SIGN and DC-SIGNR},
  author={Hadar Feinberg and Daniel Mitchell and Kurt Drickamer and William I. Weis},
  journal={Science},
  year={2001},
  volume={294},
  pages={2163 - 2166}
}
Dendritic cell specific intracellular adhesion molecule–3 (ICAM-3) grabbing nonintegrin (DC-SIGN), a C-type lectin present on the surface of dendritic cells, mediates the initial interaction of dendritic cells with T cells by binding to ICAM-3. DC-SIGN and DC-SIGNR, a related receptor found on the endothelium of liver sinusoids, placental capillaries, and lymph nodes, bind to oligosaccharides that are present on the envelope of human immunodeficiency virus (HIV), an interaction that strongly… 
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634 Citations

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Comparative analysis reveals selective recognition of glycans by the dendritic cell receptors DC-SIGN and Langerin.
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A comprehensive comparison of the glycan specificities of both proteins is described by probing a synthetic carbohydrate microarray comprising 275 sugar compounds using the bacterially produced and fluorescence-labeled, monomeric carbohydrate-recognition domains (CRDs) of DC-SIGN and Langerin.
Mannose–fucose recognition by DC-SIGN
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The structure and functions of DC-SIGN and related CTLDs in the recognition of pathogens, the molecular and structural determinants that regulate the interaction with pathogen-associated molecular patterns are focused on.
Interactions of LSECtin and DC-SIGN/DC-SIGNR with viral ligands: Differential pH dependence, internalization and virion binding
Identification of Different Binding Sites in the Dendritic Cell-specific Receptor DC-SIGN for Intercellular Adhesion Molecule 3 and HIV-1*
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This study provides a basis for the design of drugs that inhibit or alter interactions of DC-SIGN with gp120 but not with ICAM-3 or vice versa and that have a therapeutic value in immunological diseases and/or HIV-1 infections.
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Clinical strategies that target DC-SIGN may be successful in restricting HCV dissemination and pathogenesis as well as directing the migration of DCs to manipulate appropriate immune responses in autoimmunity and tumorigenic situations.
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Proteomic Analysis of DC-SIGN on Dendritic Cells Detects Tetramers Required for Ligand Binding but No Association with CD4*
TLDR
It is shown that the tetrameric complexes, in contrast to DC-SIGN monomers, bind with high affinity to high mannose glycoproteins such as mannan or HIV gp120 suggesting that such an assembly is required for high affinity binding of glycoproteinins toDC-SIGN, providing the first direct evidence that DC- Signals tetramers are essential forHigh affinity interactions with pathogens like HIV.
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References

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TLDR
Binding to clustered oligosaccharides may also explain the interaction of these receptors with the gp120 envelope protein of human immunodeficiency virus-1, which contributes to virus infection.
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DC-SIGN, a Dendritic Cell–Specific HIV-1-Binding Protein that Enhances trans-Infection of T Cells
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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