Sandra van Vliet
Cellular glycosylation is a highly dynamic process that alters upon activation, inflammation, and oncogenic transformation. Considering that 98% of all cell surface molecules are glycosylated, these glycans encompass an enormous amount of information. Within the immune system, the glycan blue prints are decoded by specific glycan-receptors, such as the C-type lectin receptors or the Siglecs. Lectins act as signaling receptors and are thus able to shape immune responses. We study how the interaction between lectin receptors and their cancer-associated glycan ligands, such as Tn antigen and the elevated levels of Sialic acids and Lewis antigens, orchestrates immune evasion during cancer progression.
Blanas A et al. Fucosylated Antigens in Cancer: An Alliance toward Tumor Progression, Metastasis, and Resistance to Chemotherapy. Front Oncol. 2018 Feb 23;8:39
Lenos K et al. MGL ligand expression is correlated to BRAF mutation and associated with poor survival of stage III colon cancer patients. Oncotarget. 2015;6(28):26278-90.
Van Kooyk Y et al. Novel insights into the immunomodulatory role of the dendritic cell and macrophage-expressed C-type lectin MGL. Immunobiology. 2015;220(2):185-92.
Van Vliet SJ et al. Human T cell activation results in extracellular signal-regulated kinase (ERK)-calcineurin-dependent exposure of Tn antigen on the cell surface and binding of the macrophage galactose-type lectin (MGL).J Biol Chem. 2013;288(38):27519-32.
Van Vliet SJ et al. MGL signaling augments TLR2-mediated responses for enhanced IL-10 and TNF-alpha secretion. J Leukoc Biol. 2013;94(2):315-23.
Van Vliet SJ et al. Regulation of effector T cells by antigen-presenting cells via interaction of the C-type lectin MGL with CD45. Nat Immunol. 2006;7(11):1200-8.
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