Similar in concept to the genome or proteome, glycome is a complete set of glycans and glycoconjugates generated by a cell or organism under specific conditions. Unlike amino acids in proteins or nucleotides in DNA, the monosaccharide units in glycan chains can be interconnected in many distinct ways, so there is no direct template or standard pattern for their biosynthesis. In addition, the structural diversity of oligosaccharide branches, the increased diversity of complex terminal saccharides, and various chemical modifications such as acetylation, phosphorylation, and sulfation, further increase the structural complexity of glycans. These great structural diversities enable glycans to encode a wide range of information, including cellular signaling, molecular recognition, and immune responses.
Identifying and analyzing the structure, quantity, and function of glycans is challenging. However, in recent years, this task has become easier with the advancement of science and technology and the continuous efforts of researchers. A variety of high-resolution and highly sensitive methods are now available, including mass spectrometry-based methods, high-performance liquid chromatography (HPLC), and lectin-based technologies.
Fig.1 Example of a glycomics and glycoproteomics analysis of an affinity purified serum glycoprotein. (Pauline, 2017)
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