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J. Biol. Chem., Vol. 281, Issue 24, 16794-16798, June 16, 2006

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All but the Shortest Polymorphic Forms of the Viral Receptor DC-SIGNR Assemble into Stable Homo- and Heterotetramers^*

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

Polymorphisms that affect the length of the extracellular neck region of the endothelial receptor DC-SIGNR (dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin-related protein) have been linked to differences in susceptibility to infection by enveloped viruses. We have characterized the effects of these polymorphisms on the ability of DC-SIGNR to form tetramers containing the clusters of sugar-binding sites needed for binding to viral envelope glycoproteins. Chemical cross-linking and analytical ultracentrifugation experiments have been used to show that only the smallest form of DC-SIGNR is defective in homotetramer assembly. A novel affinity-tagging approach has been employed to demonstrate that, contrary to previous speculation, heterotetramers can be assembled efficiently from DC-SIGNR polypeptides of different lengths. The heterotetramers are stable and can be detected in fibroblasts transfected with multiple forms of DC-SIGNR. These results provide a molecular basis for interpreting the way polymorphisms affect interactions with viruses.

Received for publication, March 15, 2006 , and in revised form, April 13, 2006.

^* This work was supported by Grant 075565 from the Wellcome Trust. 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.

¹ Recipient of a Vacation Scholarship from the Wellcome Trust.

² To whom correspondence should be addressed. Tel.: 44-20-7594-5282; E-mail: k.drickamer{at}imperial.ac.uk.

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