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Originally published In Press as doi:10.1074/jbc.M111532200 on January 17, 2002

J. Biol. Chem., Vol. 277, Issue 13, 11314-11320, March 29, 2002
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Identification of Different Binding Sites in the Dendritic Cell-specific Receptor DC-SIGN for Intercellular Adhesion Molecule 3 and HIV-1*

Teunis B. H. GeijtenbeekDagger §, Gerard C. F. van Duijnhoven, Sandra J. van VlietDagger , Elmar Krieger||, Gert Vriend||, Carl G. Figdor, and Yvette van KooykDagger

From the Dagger  Department of Molecular Cell Biology, Vrije University Medical Center Amsterdam, vd Boechorststraat 7, 1081 BT Amsterdam, The Netherlands, the  Department of Tumor Immunology and || Centre for Molecular and Biomolecular Informatics, University Medical Center Nijmegen, Geert Grooteplein Zuid 30, Nijmegen 6525 GA, The Netherlands

The novel dendritic cell (DC)-specific human immunodeficiency virus type 1 (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 intercellular adhesion molecule 3 (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.

* This research was supported by Dutch AIDS Foundation contract 5008.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed. Tel.: 31-20-4448058; Fax: 31-20-4448081; E-mail: T.Geijtenbeek.cell@med.vu.nl.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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