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Glycobiology Advance Access originally published online on June 22, 2005
Glycobiology 2005 15(11):1125-1135; doi:10.1093/glycob/cwi097
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

Mouse Siglec-F and human Siglec-8 are functionally convergent paralogs that are selectively expressed on eosinophils and recognize 6'-sulfo-sialyl Lewis X as a preferred glycan ligand

Hiroaki Tateno2, Paul R. Crocker3 and James C. Paulson1,2

2 Department of Molecular Biology, The Scripps Research Institute, San Diego, CA 92037; and 3 Division of Cell Biology and Immunology, The Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK

1 To whom correspondence should be addressed; e-mail: jpaulson{at}scripps.edu

Received on May 11, 2005; revised on June 17, 2005; accepted on June 19, 2005

Mouse sialic acid-binding immunoglobulin-like lectin F (Siglec-F) is an eosinophil surface receptor, which contains an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic domain, implicating it as a regulator of cell signaling as documented for other siglecs. Here, we show that the sialoside sequence 6'-sulfo-sLeX (Neu5Ac{alpha}2–3[6-SO4] Galß1–4[Fuc{alpha}1–3]GlcNAc) is a preferred ligand for Siglec-F. In glycan array analysis of 172 glycans, recombinant Siglec-F-Fc chimeras bound with the highest avidity to 6'-sulfo-sLeX. Secondary analysis showed that related structures, sialyl-Lewis X (sLeX) and 6-sulfo-sLeX containing 6-GlcNAc-SO4 showed much lower binding avidity, indicating significant contribution of 6-Gal-SO4 on Siglec-F binding to 6'-sulfo-sLex. The lectin activity of Siglec-F on mouse eosinophils was "masked" by endogenous cis ligands and could be unmasked by treatment with sialidase. Unmasked Siglec-F mediated mouse eosinophil binding and adhesion to multivalent 6'-sulfo-sLeX structure, and these interactions were inhibited by anti-Siglec-F monoclonal antibody (mAb). Although there is no clear-cut human ortholog of Siglec-F, Siglec-8 is encoded by a paralogous gene that is expressed selectively by human eosinophils and has recently been found to recognize 6'-sulfo-sLeX. These observations suggest that mouse Siglec-F and human Siglec-8 have undergone functional convergence during evolution and implicate a role for the interaction of these siglecs with their preferred 6'-sulfo-sLeX ligand in eosinophil biology.

Key words: 6'-sulfo-sialyl-Lewis X / eosinophils / functionally convergent paralog / Siglec-8 / Siglec-F


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