All but the shortest polymorphic forms of the viral receptor DC-SIGNR assemble into stable homo- and heterotetramers

The Journal of Biological Chemistry
Yuan GuoKurt Drickamer

Abstract

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.

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Citations

May 7, 2008·Journal of Molecular Medicine : Official Organ of the Gesellschaft Deutscher Naturforscher Und Ärzte·Ui-Soon KhooC L Steve Lin
Feb 27, 2007·Human Immunology·Luis B BarreiroLluís Quintana-Murci
Oct 20, 2009·Journal of Molecular Biology·Hadar FeinbergWilliam I Weis
Feb 11, 2020·Chemical Society Reviews·Jingying LiHuanghao Yang
May 31, 2014·Molecular Biology Reports·Ronaldo Celerino da SilvaRafael Lima Guimarães

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