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

AuthorsTabarini, Georges; Reina, José J. ; Ebel, Christine; Vivès, Corinne; Lortat-Jacob, Hughes; Rojo, Javier ; Fieschi, Franck
Surface plasmon resonance
Antiviral compound
Issue Date31-Mar-2006
PublisherFederation of European Biochemical Societies
CitationFebs Letters 580(10): 2402-2408 (2006)
AbstractDC-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.
Description7 páginas, 5 figuras. Edited by Michael R. Bubb
Publisher version (URL)http://dx.doi.org/10.1016/j.febslet.2006.03.061
Appears in Collections:(IIQ) Artículos
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