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Sialoadhesin (Sn) is an atypical siglec, due to the presence of an unusually large number of Ig domains (17) and the absence of tyrosine-based intracellular signaling motifs. Sn prefers NeuNAc in α2,3-linkage over α2,6 and α2,8 linkages but does not recognize NeuGc or NeuAc9Ac. Sn is expressed uniquely by macrophage subsets in vivo and the 17 Ig domains are thought to be important for its ability to mediate sialic acid-dependent adhesive functions. This contrasts with most other siglecs which are much shorter and masked by cis binding to co-expressed sialic acids. Sn contributes to proinflammatory immune responses in a variety of autoimmune diseases[1][2], and this may be due to suppression of Treg expansion as demonstrated in experimental allergic encephalomyelitis, a model for multiple sclerosis[3]. Sn has also been shown to function as a macrophage receptor for the porcine arterivirus[4] and can also promote macrophage uptake of sialylated bacteria such as Neisseria meningitidis[5].


CFG Participating Investigators contributing to the understanding of this paradigm

CFG Participating Investigators (PIs) contributing to the understanding of Sn include: Paul Crocker, Peter Delputte, Soerge Kelm, Ajit Varki

Progress toward understanding this GBP paradigm

Carbohydrate ligands

Cellular expression of GBP and ligands

Biosynthesis of ligands


Biological roles of GBP-ligand interaction

CFG resources used in investigations

The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the CFG database search results for sialoadhesin.

Glycan profiling

Glycogene microarray

Knockout mouse lines

Glycan array

The CFG glycan array has been probed with both murine and porcine Sn constructs, but no positive signals were obtained (click here), likely due to the low affinity of Sn for sialylated oligosaccharides.

Related GBPs



  1. Jiang, H. R. et al. Sialoadhesin promotes the inflammatory response in experimental autoimmune uveoretinitis. J Immunol 177, 2258-2264 (2006).
  2. Ip, C. W., Kroner, A., Crocker, P. R., Nave, K. A. & Martini, R. Sialoadhesin deficiency ameliorates myelin degeneration and axonopathic changes in the CNS of PLP overexpressing mice. Neurobiol Dis 25, 105-111 (2007).
  3. Wu, C. et al. Sialoadhesin-positive macrophages bind regulatory T cells, negatively controlling their expansion and autoimmune disease progression. J Immunol 182, 6508-6516 (2009).
  4. Delputte, P. L. et al. Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin. J Virol 81, 9546-9550 (2007).
  5. Jones, C., Virji, M. & Crocker, P. R. Recognition of sialylated meningococcal lipopolysaccharide by siglecs expressed on myeloid cells leads to enhanced bacterial uptake. Mol Microbiol 49, 1213-1225 (2003).


The CFG is grateful to the following PIs for their contributions to this wiki page: Paul Crocker, James Paulson

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