Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 40, Pages 34522-34532Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.243410
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Funding
- Biotechnology and Biological Sciences Research Council [BBF0083091]
- Engineering and Physical Sciences Research Council [BB/C511572/1, EP/G037604/1]
- Wellcome Trust [WT081882MA]
- Analytical Glycotechnology Core (Core C) of the Consortium for Functional Glycomics [GM 62116]
- MRC
- RCUK Basic Technology Initiative Glycoarrays [GRS/79268]
- EPSRC [EP/G037604/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/C511572/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/G037604/1, GR/S79268/02] Funding Source: researchfish
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It is well established that murine T-lymphocyte activation is accompanied by major changes in cell-surface sialylation, potentially influencing interactions with sialic acid-binding immunoglobulin-like lectins (siglecs). In the present study, we analyzed early activation of murine CD4+ and CD8+ T-lymphocytes at 24 h. We observed a striking and selective up-regulation in the binding of a recombinant soluble form of siglec-E, an inhibitory siglec, which is expressed on several myeloid cell types including antigen-presenting dendritic cells. In contrast, much lower levels of T cell binding were observed with other siglecs, including sialoadhesin, CD22, and siglec-F and the plant lectins Maackia amurensis leukoagglutinin and Sambucus nigra agglutinin. By mass spectrometry, the sialic acid content of 24-h-activated CD4+ and CD8+ T-lymphocytes exhibited an increased proportion of N-acetyl-neuraminic acid (NeuAc) to N-glycolyl-neuraminic acid (NeuGc) in N-glycans. Reduced levels of NeuGc on the surface of activated T cells were demonstrated using an antibody specific for NeuGc and the expression levels of the gene encoding NeuAc-to NeuGc-converting enzyme, CMP-NeuAc hydroxylase, were also reduced. Siglec-E bound a wide range of sialylated structures in glycan arrays, had a preference for NeuAc versus NeuGc-terminated sequences and could recognize a set of sialoglycoproteins that included CD45, in lysates from activated T-lymphocytes. Collectively, these results show that early in T cell activation, glycan remodelling involves a switch from NeuGc- to NeuAc-terminating oligosaccharides on cell surface glycoproteins. This is associated with a strong up-regulation of siglec-E ligands, which may be important in promoting cellular interactions between early activated T-lymphocytes and myeloid cells expressing this inhibitory receptor.
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