Glycans and glycan-binding proteins are central to a properly functioning immune system. Perhaps the best known example of this is the selectin family of surface proteins that are primarily found on leukocytes, and which bind to endothelial glycans near sites of infection or inflammation and enable extravasation into tissues. In the past decade, however, several other immune pathways that are dependent on or sensitive to changes in glycan-mediated mechanisms have been revealed. These include antibody function, apoptosis, T helper (Th)1 versus Th2 skewing, T cell receptor signaling, and MHC class II antigen presentation. Here, we highlight how regulated changes in protein glycosylation both at the cell surface and on secreted glycoproteins can positively and negatively modulate the immune response.
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