Mammalian glycosylation in immunity

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Abstract
Various types of mammalian extracellular glycan are produced in the secretory pathway. This Review covers the enzymatic synthesis of glycans and the mechanisms by which cellular glycans are regulated. The basic framework by which glycan structures can control molecular interactions is provided, with examples of glycoprotein conformation, glycoprotein maturation and the binding of glycan receptors known as lectins. The roles of mammalian glycans in the innate and adaptive immune systems are reviewed, as well as examples of glycan-dependent functions in the ontogeny of various immune cell types. This Review encompasses a discussion and tabulation of mammalian glycan linkages, the enzymes that produce them and their cognate recognition molecules that include lectin receptors, in the context of the immune system. The role of mammalian glycosylation in controlling the activation of intracellular phosphorylation and signal-transduction pathways is detailed. We review the molecular mechanisms that explain how the glycosylation of cell-surface molecules can govern the assembly and function of glycoprotein signalling complexes. Important outstanding questions and unexplored areas are discussed in the context of current methodologies and potential future technologies. We discuss examples of how blocking single enzymes in mammalian glycosylation can either elicit or prevent diseases of the immune system.