In contrast to nucleic acids, proteins, and lipids, glycans represent the most structurally diverse macromolecules of life. In the cell monosaccharide building blocks are assembled by glycosyltransferases into large molecules (oligo-/polysaccharides), which play important biological roles either alone or by forming glycoconjugates with proteins or lipids. Glycans are involved in cell-cell interactions, immunity, and disease progression. In the past decade, analytical approaches to decoding glycan structures, particularly the high-resolution mass spectrometry, have rapidly developed; this allows the structural characterization of glycans and glycoconjugates in detail. Glycans are recognized by glycan-binding proteins (GBPs), which include anti-glycan antibodies, different classes of lectins, membrane-bound receptors, and toxins. A GBP often binds to either one or multiple sugar residues of a glycan instead of the entire molecule. For example, the influenza hemagglutinin binds to either a2,3- or a2,6-linked sialic acids on the cell surface whereas, some selectins prefer to targeting the tetrasaccharide sialyl-Lewis X epitope abundant on O-glycans. Therefore, it is essential to define the precise structures of glyco-epitopes and to understand their biosynthetic basis.
The current knowledge on glyco-epitopes and GBPs is rather limited to the mammalian species. While the human glycome has been extensively studied, glycomes of many other organisms (e.g., parasitic worms) are less understood. As non-mammalian species have different glycosylation machineries in comparison to mammals, they synthesize glycan structures and epitopes that are immunogenic to mammals and humans. With the goal to advance our knowledge on glycans and diseases (particularly infectious diseases), we would like to encourage scientific reports on novel glycan structures/unusual epitopes, their potential binding partners and enzymes participating glycan biosynthesis. In this Research Topic, we aim to highlight the biological importance of glyco-epitopes. We encourage contributors to address the following themes:
• Review articles on defined glyco-epitopes and their receptors as well as relevant databases
• Advanced analytical approaches to determine precise glycan structures, e.g. ion mobility mass spectrometry
• Unusual carbohydrate motifs discovered in lower organisms, such as insects, fungi, plants, and marine animals
• Modern and high throughput approaches to screening novel glyco-epitopes, e.g. glycan microarrays
• Novel glycosyltransferases and glycan-modifying enzymes contributing to the biosynthesis of certain epitopes
• Glycans as novel biomarkers in the diagnosis of infectious diseases
• Novel glycan-binding proteins and their binding properties
• Studies on allergic reactions or protective immunities induced by glyco-epitopes, e.g. the a-Gal epitope
In contrast to nucleic acids, proteins, and lipids, glycans represent the most structurally diverse macromolecules of life. In the cell monosaccharide building blocks are assembled by glycosyltransferases into large molecules (oligo-/polysaccharides), which play important biological roles either alone or by forming glycoconjugates with proteins or lipids. Glycans are involved in cell-cell interactions, immunity, and disease progression. In the past decade, analytical approaches to decoding glycan structures, particularly the high-resolution mass spectrometry, have rapidly developed; this allows the structural characterization of glycans and glycoconjugates in detail. Glycans are recognized by glycan-binding proteins (GBPs), which include anti-glycan antibodies, different classes of lectins, membrane-bound receptors, and toxins. A GBP often binds to either one or multiple sugar residues of a glycan instead of the entire molecule. For example, the influenza hemagglutinin binds to either a2,3- or a2,6-linked sialic acids on the cell surface whereas, some selectins prefer to targeting the tetrasaccharide sialyl-Lewis X epitope abundant on O-glycans. Therefore, it is essential to define the precise structures of glyco-epitopes and to understand their biosynthetic basis.
The current knowledge on glyco-epitopes and GBPs is rather limited to the mammalian species. While the human glycome has been extensively studied, glycomes of many other organisms (e.g., parasitic worms) are less understood. As non-mammalian species have different glycosylation machineries in comparison to mammals, they synthesize glycan structures and epitopes that are immunogenic to mammals and humans. With the goal to advance our knowledge on glycans and diseases (particularly infectious diseases), we would like to encourage scientific reports on novel glycan structures/unusual epitopes, their potential binding partners and enzymes participating glycan biosynthesis. In this Research Topic, we aim to highlight the biological importance of glyco-epitopes. We encourage contributors to address the following themes:
• Review articles on defined glyco-epitopes and their receptors as well as relevant databases
• Advanced analytical approaches to determine precise glycan structures, e.g. ion mobility mass spectrometry
• Unusual carbohydrate motifs discovered in lower organisms, such as insects, fungi, plants, and marine animals
• Modern and high throughput approaches to screening novel glyco-epitopes, e.g. glycan microarrays
• Novel glycosyltransferases and glycan-modifying enzymes contributing to the biosynthesis of certain epitopes
• Glycans as novel biomarkers in the diagnosis of infectious diseases
• Novel glycan-binding proteins and their binding properties
• Studies on allergic reactions or protective immunities induced by glyco-epitopes, e.g. the a-Gal epitope