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J. Biol. Chem., Vol. 281, Issue 29, 20440-20449, July 21, 2006

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Widely Divergent Biochemical Properties of the Complete Set of Mouse DC-SIGN-related Proteins^*

From the Division of Molecular Biosciences, Imperial College, London SW7 2AZ, United Kingdom

The mouse genome sequence has been examined to identify the complete set of proteins related to the human glycanbinding receptor, DC-SIGN. In addition to five SIGNR proteins previously described, a pseudogene, encoding a hypothetical SIGNR6, and a further two expressed proteins, SIGNR7 and SIGNR8, have been identified. The ligand-binding properties of these novel proteins and of the previously described mouse SIGNs have been systematically investigated in order to define the mouse proteins that most resemble human DC-SIGN and DC-SIGNR. Results from screening of a glycan array demonstrate that only mouse SIGNR3 shares with human DC-SIGN the ability to bind both high mannose and fucose-terminated glycans in this format and to mediate endocytosis. The finding that neither SIGNR1 nor SIGNR5 binds with high affinity to specific ligands in a large panel of mammalian glycans is consistent with the suggestion that these receptors bind surface polysaccharides on bacterial and fungal pathogens in a manner analogous to serum mannose-binding protein. The data also reveal that two of the mouse SIGNs have unusual binding specificities that have not been previously described for members of the C-type lectin family; the newly identified SIGNR7 binds preferentially to the 6-sulfo-sialyl Lewis^x oligosaccharide, whereas SIGNR2 binds almost exclusively to glycans that bear terminal GlcNAc residues. The results presented demonstrate that the mouse homologs of DC-SIGN have a diverse set of ligand-binding and intracellular trafficking properties, some of which are distinct from the properties of any of the human receptors.

Received for publication, February 28, 2006 , and in revised form, April 27, 2006.

^* This work was supported by Wellcome Trust Grant 075565 and National Institutes of Health Grant GM62116 (to the Consortium for Functional Glycomics). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The online version of this article (available at http://www.jbc.org) contains supplemental Tables 1 and 2.

¹ These authors contributed equally to this work.

² Recipient of a Vacation Scholarship from the Wellcome Trust.

³ To correspondence should be addressed: Division of Molecular Biosciences, Biochemistry Bldg., Imperial College, London SW7 2AZ, United Kingdom. Tel.: 44-20-7594-5282; E-mail: k.drickamer{at}imperial.ac.uk.

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