Mannose hyperbranched dendritic polymers interact with clustered organization of DC-SIGN and inhibit gp120 binding

FEBS Lett. 2006 May 1;580(10):2402-8. doi: 10.1016/j.febslet.2006.03.061. Epub 2006 Mar 31.

Abstract

DC-SIGN (dendritic cell-specific ICAM-3 grabbing non-integrin) is a C-type lectin receptor of dendritic cells and is involved in the initial steps of numerous infectious diseases. Surface plasmon resonance has been used to study the affinity of a glycodendritic polymer with 32 mannoses, to DC-SIGN. This glycodendrimer binds to DC-SIGN surfaces in the submicromolar range. This binding depends on a clustered organization of DC-SIGN mimicking its natural organization as microdomain in the dendritic cells plasma membrane. Moreover, this compound inhibits DC-SIGN binding to the HIV glycoprotein gp120 with an IC50 in the micromolar range and therefore can be considered as a potential antiviral drug.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biopolymers / chemistry*
  • Biopolymers / pharmacology
  • Cell Adhesion Molecules / chemistry*
  • Cell Adhesion Molecules / metabolism
  • HIV Envelope Protein gp120 / drug effects*
  • HIV Envelope Protein gp120 / metabolism
  • Lectins, C-Type / chemistry*
  • Lectins, C-Type / metabolism
  • Mannose / chemistry*
  • Molecular Structure
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / metabolism
  • Solutions

Substances

  • Biopolymers
  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • HIV Envelope Protein gp120
  • Lectins, C-Type
  • Receptors, Cell Surface
  • Solutions
  • Mannose