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In recent years, it has become increasingly clear that glycosylation of key pathogen glycoprotein antigens can significantly affect antigenic properties. For example, pathogens, such as human immunodeficiency virus and influenza, can develop a ‘glycoshield’ over key antigens as they passage through host populations. In addition to shielding of antigenic sites key changes in glycosylation have been shown to modify host innate immune responses and both of these phenomena can potentially impact vaccine performance. A better understanding of glycosylation properties of vaccine antigens may better guide development of these products and management of their production processes. Due to the complexity of oligosaccharides, the analysis of these glycosylation states has been difficult and time consuming. With the advent of cutting edge mass spectrometry based techniques many of the barriers to glycan and glycoprotein analysis have been lowered. Combined with traditional techniques such as high field NMR, GC/MS, CE...
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