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M111532200v1
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Papers In Press, published online ahead of print January 17, 2002
J. Biol. Chem, 10.1074/jbc.M111532200
Submitted on December 4, 2001
Revised on January 15, 2002
Accepted on January 16, 2002

Identification of different binding sites in the dendritic cell-specific receptor DC-sIGN for ICAM-3 and HIV-1

Teunis B.H. Geijtenbeek, Gerard C.F. van Duijnhoven, Sandra J. van Vliet, Elmar Krieger, Gert Vriend, Carl G. Figdor, and Yvette van Kooyk

Department of Molecular Cell Biology, Vrije University Medical Center Amsterdam, Amsterdam 1081 BT

Corresponding Author: T.Geijtenbeek.Cell{at}med.vu.nl

The novel dendritic cell (DC)-specific HIV-1 receptor DC-SIGN plays a key-role in the dissemination of HIV-1 by DC. DC-SIGN is thought to capture HIV-1 at mucosal sites of entry, facilitating transport to lymphoid tissues where DC-SIGN efficiently transmits HIV-1 to T cells. DC-SIGN is also important in the initiation of immune responses by regulating DC-T cell interactions through ICAM-3. We have characterized the mechanism of ligand binding by DC-SIGN and identified the crucial amino acids involved in this process. Strikingly, the HIV-1 gp120 binding site in DC-SIGN is different from that of ICAM-3, consistent with the observation that glycosylation of gp120, in contrast to ICAM-3, is not crucial to the interaction with DC-SIGN. A specific mutation in DC-SIGN abrogated ICAM-3 binding whereas the HIV-1 gp120 interaction was unaffected. This DC-SIGN mutant captured HIV-1 and infected T cells in trans as efficiently as wild-type DC-SIGN, demonstrating that ICAM-3 binding is not necessary for HIV-1 transmission. This study provides a basis for the design of drugs that inhibit or alter interactions of DC-SIGN with gp120 but not with ICAM-3, or vice versa, and that have a therapeutic value in immunological diseases and/or HIV-1 infections.


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