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License: Licence agreement concerning inclusion of doctoral thesis in the Institutional Repository of the University of LeidenN/A • February 7th, 2023
This is particularly poignant in immunology, where protein glycosylation plays a major role in many key processes, like regulation of immunotolerance,3,4 uptake of antigens5,6, the creation of neo-epitopes7,8, and even the protection of the foetus.9 The precise study of these processes has been hampered by a dearth of well-defined reagents. In some cases, well- defined glycans, in the absence of any protein scaffold, can be used to study these functions. For instance, the carbohydrate binding specificity of many lectins have been determined using synthetic oligosaccharides in absence of a protein scaffold.10,11 However, for many processes, the combination of carbohydrate and protein is key. For example, antigen (cross-)presentation is thought to be enhanced by uptake of the antigen via lectins12,13 and therefore requires a covalent attachment of the protein and the (specific) oligosaccharide.
