• My NEB
  • Print
  • PDF
  • Glycobiology

    Glycobiology is the study of the structure, function and biology of carbohydrates, often called glycans, which are widely distributed in nature (1). It is a small but rapidly growing field in biology, with relevance to biomedicine, biotechnology, biofuels and basic research. In eukaryotic cells the majority of proteins are post-translationally modified (2). A common modification, essential for cell viability, is the attachment of glycans. For a visual representation, see the N-linked and O-linked glycosylation tab below.

    Glycans define many properties of glycoconjugates (glycoproteins and glycolipids). For instance, it is largely through glycan–protein interactions that cell–cell and cell–pathogen contacts occur. Likewise, glycan molecules modulate many other processes important for cell and tissue differentiation, metabolic and gene regulation, protein activity, protein clearance, transport, and more (3-10). For more information, see the role of carbohydrates in the inflammation response tab below.

    References

    1. Spiro, R. G. (2002) Glycobiology 12, 43R-56R. PMID: 112042244
    2. Khoury G.A. et al (2011) Scientific Reports 1: 90. PMID: 22034591
    3. Varki A. (1993) Glycobiology. 3(2):97-130. PMID: 8490246
    4. Zhao Y.Y. et al (2008) Cancer Sci. 99(7):1304-10. PMID: 18492092
    5. Zhao Y. et al (2008) FEBS J. 275(9):1939-48. PMID: 18384383
    6. Skropeta D. (2009) Bioorg Med Chem. 17(7):2645-53. PMID: 19285412
    7. Neu U. et al (2011) Curr Opin Struct Biol. 21(5):610-8. PMID: 21917445
    8. Cerliani J.P. et al (2011) J Clin Immunol. 31(1):10-21. PMID: 21184154
    9. Aarnoudse C.A. et al (2006) Curr Opin Immunol. 18(1):105-11. PMID: 16303292
    10. Arnold J.N. (2006) Immunol Lett. 106(2):103-10. PMID: 16814399
    • Overview of Glycobiology

      Learn about the core sequences and common modifications of N-linked and O-linked glycans in this video. Analysis of these glycans and/or peptide portions of the glycoprotein can be accomplished with the use of deglycosylation enzymes, which are explained in detail. Unlike other chemical deglycosylation methods, enzymatic treatment is much gentler and can provide complete sugar removal with no protein degradation.

      scroll to see additional videos
    • Identification and Characterization of Protein Glycosylation

      Here we illustrate the use of glycosidases for the analysis of a model glycoprotein: recombinant human chorionic gonadotropin beta (hCGβ), which carries both N-glycans and O-glycans in this video. The technique requires only simple instrumentation and typical consumables, and it can be readily adapted to the analysis of multiple glycoprotein samples.

      scroll to see additional videos
    • Elucidating the Complexity of Heparin Oligosaccharide Analysis

      Learn more about the structural elucidation of complex and diverse heparin oligosaccharides using Bacteroides Heparinase I, II and III in combination with downstream mass spec analysis.

      scroll to see additional videos

    Glycobiology includes these areas of focus:

    Sequencing Glycans
    Biosynthesis of Glycans in Eukaryotes
    Removal of N-Linked & O-Linked Glycans from Glycoproteins
    Glycoprotein Production in Various Expression Systems
    Depolymerization of Heparin/HS
    MS Analysis of GAGs

    FAQs for Glycobiology

      Publications related to Glycobiology:

    1. Wong-Madden, S.T., Landry, D., and Guthrie, E.P. (1997) Discovery and Uses of Novel Glycosidases Techniques in Glycobiology 401-408.
    2. Wagner-Rousset, E., Bednarczyk, A., Bussat, M.C., Colas, O., Corvaïa, N., Schaeffer, C., Van Dorsselaer, A., Beck, A. (2008) The way forward, enhanced characterization of therapeutic antibody glycosylation: comparison of three level mass spectrometry-based strategies J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 872, 23-37. PubMedID: 18672411
    3. Graham, D.R., Mitsak, M.J., Elliott, S.T., Chen, D., Whelan, S.A., Hart, G.W., Van Eyk, J.E. (2008) Two-dimensional gel-based approaches for the assessment of N-Linked and O-GlcNAc glycosylation in human and simian immunodeficiency viruses Proteomics 8, 4919-30. PubMedID: 19072736
    4. Rasmussen, T.N., Plenge, P., Bay, T., Egebjerg, J., Gether, U. (2009) A single nucleotide polymorphism in the human serotonin transporter introduces a new site for N-linked glycosylation Neuropharmacology 57, 287-94. PubMedID: 19500602
    5. Gong, B., Cukan, M., Fisher, R., Li, H., Stadheim, T.A., Gerngross, T. (2009) Characterization of N-linked glycosylation on recombinant glycoproteins produced in Pichia pastoris using ESI-MS and MALDI-TOF Methods Mol. Biol. 534, 213-23.
    6. Gefter, J.V., Shaufl, A.L., Fink, M.P., Delude, R.L. (2009) Comparison of distinct protein isoforms of the receptor for advanced glycation end-products expressed in murine tissues and cell lines Cell Tissue Res. 337, 79-89. PubMedID: 19415334
    7. Boeggeman, E., Ramakrishnan, B., Pasek, M., Manzoni, M., Puri, A., Loomis, K.H., Waybright, T.J., Qasba, P.K. (2009) Site specific conjugation of fluoroprobes to the remodeled Fc N-glycans of monoclonal antibodies using mutant glycosyltransferases: application for cell surface antigen detection Bioconjug. Chem. 20, 1228-36. PubMedID: 19425533
    8. Velho, A.M., Jarvis, S.M. (2009) Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting Exp. Cell Res. 315, 2312-21. PubMedID: 19379732

    N-Linked and O-Linked Glycosylation

    N-linked glycosylation occurs through consensus asparagine residues of the protein, while O-glycosylation occurs through serine or threonine residues.