4.5 Article

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

Journal

FEBS LETTERS
Volume 580, Issue 10, Pages 2402-2408

Publisher

WILEY
DOI: 10.1016/j.febslet.2006.03.061

Keywords

carbohydrates; DC-SIGN; gp120; multivalency; surface plasmon resonance; antiviral compound

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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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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