Second generation of fucose-based DC-SIGN ligands: affinity improvement and specificity versus Langerin

Org Biomol Chem. 2011 Aug 21;9(16):5778-86. doi: 10.1039/c1ob05573a. Epub 2011 Jul 7.

Abstract

DC-SIGN and Langerin are two C-type lectins involved in the initial steps of HIV infections: the former acts as a viral attachment factor and facilitates viral invasion of the immune system, the latter has a protective effect. Potential antiviral compounds targeted against DC-SIGN were synthesized using a common fucosylamide anchor. Their DC-SIGN affinity was tested by SPR and found to be similar to that of the natural ligand Lewis-X (Le(X)). The compounds were also found to be selective for DC-SIGN and to interact only weakly with Langerin. These molecules are potentially useful therapeutic tools against sexually transmitted HIV infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-HIV Agents / chemistry
  • Anti-HIV Agents / pharmacology
  • Antigens, CD / metabolism
  • Cell Adhesion Molecules / antagonists & inhibitors*
  • Cell Adhesion Molecules / metabolism*
  • Fucose / chemistry*
  • Fucose / pharmacology*
  • HIV Infections / drug therapy
  • Humans
  • Lectins, C-Type / antagonists & inhibitors*
  • Lectins, C-Type / metabolism*
  • Mannose-Binding Lectins / metabolism
  • Models, Molecular
  • Protein Binding
  • Receptors, Cell Surface / antagonists & inhibitors*
  • Receptors, Cell Surface / metabolism*

Substances

  • Anti-HIV Agents
  • Antigens, CD
  • CD207 protein, human
  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • Lectins, C-Type
  • Mannose-Binding Lectins
  • Receptors, Cell Surface
  • Fucose