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

Georges Tabarani (1) , José J Reina , Christine Ebel (1) , Corinne Vivès (1) , Hugues Lortat-Jacob (1) , Javier Rojo (2) , Franck Fieschi (1)

1 IBS - UMR 5075 - Institut de biologie structurale
2 Glycosystems Laboratory

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.

Domaines: Biochimie, Biologie Moléculaire

Georges Tabarani, José J Reina, Christine Ebel, Corinne Vivès, Hugues Lortat-Jacob, et al.. Mannose hyperbranched dendritic polymers interact with clustered organization of DC-SIGN and inhibit gp120 binding.. FEBS Letters, 2006, 580 (10), pp.2402-8. ⟨10.1016/j.febslet.2006.03.061⟩. ⟨hal-01062655⟩