1. Concepts of glycobiology -- 1.1. The field of glycobiology encompasses the multiple functions of sugars attached to proteins and lipids -- 1.2. There are three major classes of glycoconjugates -- 1.3. Glycans are composed of monosaccharides with related chemical structures -- 1.4. Glycosidic linkages between monosaccharides exist in multiple configurations -- 1.5. Formation of glycosidic linkages requires energy and is catalysed by specific enzymes -- 1.6. Understanding structure-function relationships for glycans can be more difficult than for other classes of biopolymers -- 1.7. Glycan structures are encoded indirectly in the genome

2. N-linked glycosylation -- 2.1. Diverse N-linked glycans have a common core structure -- 2.2. Assembly of N-linked glycans occurs in three major stages -- 2.3. The precursor oligosaccharide for N-linked glycans is assembled on the lipid dolichol -- 2.4. The dolichol-linked precursor oligosaccharide is transferred to asparagine residues of polypeptides -- 2.5. The core oligosaccharide structure is modified by glycosidases and glycosyltransferases -- 2.6. Hybrid structures and polylactosamine sequences are common extensions of the core oligosaccharide -- 2.7. ABO blood groups are determined by the presence of different terminal sugars on glycans of red blood cells -- 2.8. Hundreds of glycosyltransferases generate highly diverse N-linked glycans -- 2.9. The N-linked glycans of an individual glycoprotein are usually heterogeneous -- 2.10. The nature of N-linked glycans attached to an individual glycoprotein is determined by the protein and the cell in which it is expressed -- 2.11. High mannose structures are present in lower eukaryotes, but the glycosylation machinery has evolved to produce complex glycans in higher organisms -- 2.12.e lipid dolichol -- 2.4.
N-linked glycans are essential for development of multicellular organisms --

3. Conformations of oligosaccharides -- 3.1. Three-dimensional structures of oligosaccharides are called conformations -- 3.2. Monosaccharides assume a limited number of conformations -- 3.3. Torsion angles are used to describe conformations of glycans -- 3.4. Local steric and electronic interactions limit the possible conformations of glycosidic linkages -- 3.5. The conformation of an oligosaccharide is influenced by interactions between hexoses distant from each other in the covalent structure -- 3.6. Co-operative interactions determine the overall folds of oligosaccharides -- 3.7. Oligosaccharide conformations are dynamic -- 3.8. Short- and long-range interactions also determine the conformations of polysaccharides -- 3.9. The conformations of a small number of oligosaccharides have been analysed by X-ray crystallography and nuclear magnetic resonance

4. Strategies for analysis of glycan structures -- 4.1. Enzymes are used to analyses structures of N-linked glycans -- 4.2. Isolated oligosaccharides and intact glycoconjugates can be analysed with lectins -- 4.3. Mass spectrometry and nuclear magnetic resonance spectroscopy are useful physical methods for establishing glycan structures -- 4.4. Small oligosaccharides can be synthesized using chemical methods -- 4.5. Enzymes provide an alternative method for the synthesis of oligosaccharides -- 4.6. Neoglycoconjugates can be created by chemically linking sugars to proteins or lipids

5. O-linked glycosylation -- 5.1. Mucins are large, heavily O-glycosylated proteins that hold water -- 5.2. Some cell surface proteins have mucin-like domains -- 5.3. Many soluble and cell surface glycoproteins contain small clusters of O-linked sugars -- 5.4. Biosynthesis of mucin-type sugars occurs by sequential addition of monosaccharides to proteins in the Golgi apparatus -- 5.5. Proteoglycans are heavily O-glycosylated proteins that give strength to the extracellular matrix -- 5.6. Cell surface proteoglycans interact with growth factors -- 5.7. Biosynthesis of proteoglycans requires several modifying enzymes in addition to glycosyltransferases -- 5.8. O-linked fucose-based glycans are important for extracellular signalling during development -- 5.9. Unusual types of O-linked glycosylation are found on some proteins -- 5.10. Cytoplasmic and nuclear proteins can be modified by addition of O-linked N-acetylglucosamine

6. Glycolipids and membrane protein glycosylation -- 6.1. Most integral membrane proteins are glycosylated -- 6.2. Polysialylation of neural cell adhesion molecule prevents cell adhesion -- 6.3. Membranes contain glycolipids as well as glycoproteins -- 6.4. Glycosphingolipid biosynthesis occurs in the Golgi apparatus -- 6.5. Cell surface glycolipids are important for the development of the nervous system -- 6.6. Defects in glycolipid breakdown cause disease -- 6.7. Some proteins are attached to membranes through glycolipid anchors -- 6.8. Glycolipid anchors are added to proteins in the endoplasmic reticulum -- 6.9. Proteins attached to glycolipid anchors are localized to the plasma membrane -- 6.10. The disease paroxysmal nocturnal haemoglobinuria is caused by a glycolipid anchor deficiency

7. Effects of glycosylation on protein structure and function -- 7.1. Various approaches can be used to study the effects of glycosylation -- 7.2. Sugars stabilize the structure of the cell adhesion molecule CD2 -- 7.3. An oligosaccharide replaces an [alpha]-helix in some variant surface glycoproteins of trypanosomes -- 7.4. Attachment of a monosaccharide can increase protein stability -- 7.5. The stability of ribonuclease is increased by N-glycosylation -- 7.6. Protein-protein interactions can be modulated by oligosaccharides -- 7.7.n glycolipid breakdown cause disease -- 7.8. Oligosaccharides covering surfaces can protect against proteolysis

8. Glycoprotein trafficking in cells and organisms -- 8.1. Animal lectins have diverse structures and functions -- 8.2. Lectins have important functions in the secretory pathway -- 8.3. Calnexin and calreticulin help glycoproteins fold in the endoplasmic reticulum -- 8.4. Lectins are involved in degradation of misfolded glycoproteins -- 8.5. L-type lectins transport glycoproteins from the endoplasmic reticulum to the Golgi -- 8.6. Mannose 6-phosphate residues target lysosomal enzymes to lysosomes -- 8.7. Two types of mannose 6-phosphate receptor take part in lysosomal enzyme targeting -- 8.8. The asialoglycoprotein receptor clears altered serum glycoproteins into the liver -- 8.9. The mannose receptor removes naturally occurring glycoproteins from circulation -- 8.10. The mannose receptor also regulates activity of sulphated hormones -- 8.11. Some intracellular lectins have roles in the nucleus

9. Carbohydrate recognition in cell adhesion and signalling -- 9.1. The selectins are cell adhesion molecules for white blood cells -- 9.2. Specific carbohydrate ligands for the selectins have been identified -- 9.3. The selectins are also signal transduction molecules -- 9.4. C-type lectins participate in the process of antigen presentation -- 9.5. DC-SIGN and DC-SIGNR enhance human immunodeficiency virus infection of T cells -- 9.6. The siglecs are cell adhesion and signalling molecules -- 9.7. Sialoadhesin is an adhesion receptor on macrophages -- 9.8. Myelin-associated glycoprotein has roles in the central and peripheral nervous systems -- 9.9. CD22 is a signalling molecule on B cells -- 9.10. Extracellular galectins have roles in cell adhesion and cell signalling -- 9.11. Mannose-binding protein is a host defence molecule -- 9.12. Mannose-binding protein initiates the lectin pathway of complement activation -- 9.13. The mannose receptor helps macrophages to internalize pathogens

10. Mechanisms of sugar recognition in animal lectins --
10.1. Lectin classification is based on primary structure -- 10.2. C-type carbohydrate-recognition domains bind two hydroxyl groups of a monosaccharide in complex with Ca[superscript 2] -- 10.3. A small number of residues in a C-type carbohydrate-recognition domain determines the types of ligand that are bound -- 10.4. Some features of monosaccharide binding are similar in all types of carbohydrate-recognition domains -- 10.5. Binding of oligosaccharide ligands to the selectins requires additional interactions with the carbohydrate-recognition domains -- 10.6. Extended binding sites are found in many lectins -- 10.7. Valency and oligomer geometry determine specificity and affinity of lectins for oligosaccharides

11. Glycobiology of plants, bacteria, and viruses -- 11.1. Plant and microbial glycans have some functions not seen in mammals -- 11.2. Plants use oligosaccharides as signalling molecules -- 11.3. Common plant lectins are useful tools for biologists -- 11.4. Some plant lectins are toxins -- 11.5. Many bacterial toxins are lectins -- 11.6. Bacteria use lectins to bind to host cell surfaces -- 11.7. Viruses use lectins to target cell surfaces -- 11.8. Lectins appeared early in evolution but have diverse functions in higher organisms

12. Glycosylation and disease -- 12.1. Mutations in enzymes for synthesis of N-linked glycans cause congenital disorders of glycosylation -- 12.2. Abnormal expression of a glycosyltransferase causes a blood clotting defect -- 12.3. Chemical glycation of proteins occurs in diabetes -- 12.4. Antibodies to carbohydrates can cause disease -- 12.5. IgG glycosylation is altered in rheumatoid arthritis -- 12.6. Changes in glycosylation are associated with cancer

13.1. Important clues about roles for specific glycans will continue to come from biochemical and genetic studies -- 13.2. Genomics is starting to provide new insights into glycobiology -- 13.3. Glycomics promises a global view of glycobiology -- 13.4. Model organisms will be most useful in the analysis of more primitive functions of glycosylation -- 13.5. Molecular understanding of how glycans function will require further elucidation of structure - function relationships -- 13.6. Our increasing knowledge about glycobiology is being applied to practical issues.