Glycans in Genetic Disorders

Carbohydrates were prominent in the early history of immunology in defining the identity of antigens recognized by antibodies. In addition, the ability of antibodies to specifically recognize glycans was exploited in studies defining the size of the antigen-binding site. Nevertheless, for many decades following these early discoveries the broader potential importance of carbohydrates in both innate and adaptive immune responses was largely overlooked. However, times are changing and glycobiologists and immunologists are now collaborating extensively to explore this very fertile area of immunobiologyNumerous carbohydrate-binding proteins, or lectins, have been identified on the surfaces of immune cells. Interactions of lectins with glycans usually require several monosaccharide moieties presented in the correct conformation for high-affinity binding. Modification of proteins and lipids by glycosylation is a highly regulated process resulting in a diverse repertoire of glycan structures.

Glycans are at the center of many disorders and diseases sparking the possibility of exploiting them for therapeutic and diagnostic purposes. There are many biochemical pathways and diseases in which glycans are intricately involved. Gaging the vast potential and the promise that glycobiology holds, many pharma and biotech companies have already started allocating their R&D budget to it. Presently, with our drug arsenal fast depleting against drug resistant and mutant pathogens, glycobiology hold an untapped source of new candidate drugs.

Relevant Conferences: Glycobiology Conferences Biochemistry Conferences

7th International Conference on Bioinformatics, October 24-26, 2016 Rome, Italy; International Conference on Structural Biology, August 22-23, 2016 New Orleans, USA; International Conference on Glycomics, December 01-02, 2016 Atlanta, Georgia, USA; International Conference on Nucleic Acids, August 04-05, 2016 New Orleans, Louisiana, USA; 2nd International Conference on Transcriptomics, September 12-14, 2016 Philadelphia, Pennsylvania, USA; International Conference on Obesity & Chronic Diseases, July 25-27, 2016 Las Vegas USA; International Conference on New Therapeutics for Diabetes and Obesity, April 17-20, 2016 La Jolla, USA; Conference on Plasma Spectrochemistry, January 10-16, 2016 Tucson, USA; Euro Fed Lipid Congress, September 18-21, 2016 Gent, Belgium; Conference on Obesity and Adipose Tissue Biology, February 15-19, 2016 Banff, Canada; Society for Glycobiology, November 19-22, 2016 New Orleans, Louisiana, USA; American Society for Biochemistry and Molecular Biology (ASBMB), April 02-06, 2016 San Diego, USA; Federation of American Societies for Experimental Biology (FASEB), June 12-17, 2016 Florida, USA

Carbohydrates are capable of generating structural diversity in multiple ways and are prominently displayed on the surfaces of cell membranes or on the exposed regions of macromolecules. Unlike proteins, which are connected solely by a peptide bond, carbohydrates utilize many possible glycosidic linkages so as to extensively diversify their structures. Glycosylation is a critical function of the biosynthetic-secretory pathway in the endoplasmic reticulum (ER) and Golgi apparatus. Glycosylation increases the diversity of the proteome to a level unmatched by any other post-translational modification. Glycosidases catalyze the hydrolysis of glycosidic bonds to remove sugars from proteins. These enzymes are critical for glycan processing in the ER and Golgi, and each enzyme shows specificity for removing a particular sugar (e.g., mannosidase).

  • Translational diagnostics
  • Tools and technologies for single cell analysis
  • The impact of genomic variation in clinical developmeni
  • Application and related disorders
  • Biochemical diagnostics

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