Image shows complex glycan structure with N-acetylglucosamine, mannose, galactose, N-Acetylneuraminic acid, fucose.

Glycobiology is the study of the biosynthesis, structure, function, and evolution of glycans and glycoconjugates. Studying the dynamic changes in glycan and glycoconjugate profiles is essential to understand key biological processes in organisms. The human immune system largely functions via glycan-protein interactions. The physiology and pathogen recognition of glycoproteins, glycolipids and carbohydrates are being studied for next-generation therapeutics, vaccines, and diagnostics for cancer and autoimmune diseases.

The carbohydrate moieties of cell surface glycoproteins and glycolipids function in cellular communication processes and physiological responses. Cell-surface glycoproteins and glycolipids provide anchors for intercellular adhesion and points of attachment for antibodies and other proteins, and function as receptor sites for bacteria and viruses. Altered cell surface glycosylation patterns are associated with cellular differentiation, development, viral infection, and are diagnostic in certain cancers, seven of them correlating to changes in the expression or localization of relevant glycosyltransferases.

Common applications are glycomics and glycoproteomics research fields. They include areas such as glycan synthesis, glycosylation and deglycosylation, and glycan analysis. Glycomics is a subset field of glycobiology that aims to identify the structure and function of glycans or the glycome in a cell or organism. Glycoproteomics is focused on determining the positions and identities of glycans in glycoproteins in cells or tissues. Mass spectroscopy is widely used in both glycomics and glycoproteomics fields of study, but analysis is still very challenging due to the diversity of glycans and the variations of glycosylation sites.

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