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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

Academic Article
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Overview

authors

  • Tateno, H.
  • Crocker, P. R.
  • Paulson, James

publication date

  • November 2005

journal

  • Glycobiology  Journal

abstract

  • 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-sLe(X) (Neu5Acalpha2-3[6-SO4] Galbeta1-4[Fucalpha1-3]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-sLe X. Secondary analysis showed that related structures, sialyl-Lewis X (sLe X) and 6-sulfo-sLe X containing 6-GlcNAc-SO4 showed much lower binding avidity, indicating significant contribution of 6-Gal-SO4 on Siglec-F binding to 6'-sulfo-sLe x. 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-sLe X 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-sLe X. 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-sLe X ligand in eosinophil biology.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Antigens, CD
  • Antigens, Differentiation, B-Lymphocyte
  • Antigens, Differentiation, Myelomonocytic
  • CHO Cells
  • Cricetinae
  • Eosinophils
  • Humans
  • Lectins
  • Ligands
  • Mice
  • Mice, Transgenic
  • Microscopy, Fluorescence
  • Neuraminidase
  • Oligosaccharides
  • Polysaccharides
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Research

keywords

  • 6 '-sulfo-sialyl-Lewis X
  • Siglec-8
  • Siglec-F
  • eosinophils
  • functionally convergent paralog
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Identity

International Standard Serial Number (ISSN)

  • 0959-6658

Digital Object Identifier (DOI)

  • 10.1093/glycob/cwi097

PubMed ID

  • 15972893
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Additional Document Info

start page

  • 1125

end page

  • 1135

volume

  • 15

issue

  • 11

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