Glycobiology of the Immune System and Disease

Dr. Shyamasree Ghosh (MSc, PhD, PGDHE, PGDBI) has worked and published extensively in glycobiology, biology of sialic acids, immunology, stem cells, nanotechnology and computational biology and is currently working as the Scientific Officer, since 2009 in the School of Biological Sciences, National Institute of Science Education and Research (NISER), Bhubaneswar, under Department of Atomic Energy, Govt of India currently located in Jatni, Orissa. ty. She has authored several publications that include books and encyclopedia chapters in reputed journals and books. Research that tries to decode the complexity of life with hopes for a better living forms her research interest.

• 1. Glycans of the immune system1.1 Immune system1.2 Glycans1.3 Glycosylation1.4 Glycan-binding proteins (GBPs) or lectins2. C-type lectin in host-pathogen interactions2.1 Structure2.2 C-type lectin receptors and infection biology3. Galectins3.1 Introduction3.2 Role in infection4. Siglecs and the immune system4.1 Sialic acid recognition by siglecs and cis interactions with endogenous glycans4.2 Sialoadhesin and cellular interactions in the immune system5. CD22 and B cell signalling6. New CD33-related Siglecs in the innate immune system7. Modulation of immune tolerance by Siglec-sialic acid interaction8. Siglecs and immune regulation8.1 Pathogen internalization by innate immune cells: phagocytosis and endocytosis by Siglec9. Siglecs and the attenuation of inflammatory responses9.1 Immune evasion by pathogens via Siglec ligation9.2 Attenuation of DAMP-mediated inflammation by Siglecs10. The regulation of the life span of myeloid cells in the context of inflammation by Siglec-8, Siglec-9, and Siglec-F10.1 Regulation of natural killer cell function by Siglec-711. Siglecs, dendritic cells, and T cell activation11.1 Siglecs and the regulation of plasmacytoid dendritic cell function11.2 Siglecs in conventional dendritic cells and the regulation of T cell activation and polarization11.3 A direct role for Siglecs in T cells11.4 Siglecs in B cell biology and the maintenance of immunological tolerance12. Glycobiology of autoimmunity and chronic inflammation13. Immune response and glycobiology13.1 Glycobiology of pathogens13.2 Role of glycan-binding proteins14. Glycobiology of fungus and infection14.1 Pathogenic fungi14.2 Candida albicans: glycans are central in host interactions14.3 Aspergillus fumigatus14.4 Cryptococcus neoformans and its capsule14.5 Fungal glycans and drug targets15. Glycobiology of virus and infection15.1 Zika virus15.2 Coronavirus and COVID-1915.3 Lassa15.4 Mumps15.5 Chlorella15.6 Varicella zoster15.7 Avian coronavirus15.8 Influenza A virus15.9 Chikungunya virus15.10 Semliki Forest virus15.11 Herpes simplex virus (HSV)15.12 Rabies virus15.13 Rotavirus15.14 Ross river virus15.15 H1N1/H5N1 virus15.16 New Castle disease virus16. Glycans as antibody epitopes17. Glycobiology of bacteria and infection17.1 Bacterial surface glycans as virulence factors17.1.1 Polysaccharide capsules17.1.2 Lipopolysaccharide (LPS)17.2 Mechanisms of colonization and invasion17.2.1 Adhesins and receptors17.2.2 Invasion factors17.3 Bacterial toxins as glycosyltransferases17.4 Glycan-based interaction of host and gut microflora: commensals and pathogens18. Glycobiology of tumour and immunity18.1 Glycosylation in cancer18.1.1 Altered branching and fucosylation of N-glycans18.1.2 Increased mucins and truncated O-glycans18.1.3 Increased and aberrant sialic acid expression18.1.4 Increased selectin ligand expression18.2 Altered expression of blood groups18.3 Altered expression of glycosphingolipids18.4 Loss of GPI-anchor expression18.5 Altered hyaluronan18.6 Alterations in sulfated glycosaminoglycans18.7 Altered cytoplasmic and nuclear O-GlcNAc18.8 Mechanisms of altered glycan expression18.9 Glycan changes in cancer stem cells and during EMT18.10 Clinical significance19. Therapeutic strategies based on microorganism and virus protein-glycan interactions19.1 Structure–function considerations of glycans19.2 Pharmacological driving force: protein–GAG interactions and the glycan-protein network (GPN)19.3 Identification of protein-specific GAG sequences19.4 Therapeutic approaches